Journal of Virology · 2003 · 62 citations · 43 references
Life SciencesMicrobiologyMolecular BiologyMedical MicrobiologyMolecular VirologyVirologyGlycan StructureGlycan-protein InteractionsProtein GlycosylationViral InfectionsViral Protein ProcessingViral StructureGlycoprotein StructureHigh-mannose GlycansHigh-mannose N-glycansHuman Herpesvirus 6 InfectionViral Entry ComplexesViral Entry ReceptorsViral GlycoproteinsViral Protein Glycosylation
The human herpesvirus 6 (HHV-6) variant A U100 gene encodes the third component of the glycoprotein H (gH)-glycoprotein L (gL)-containing complex. Glycosidase digestion analysis showed that the U100 gene products are glycoproteins consisting of an 80-kDa protein with complex N-linked oligosaccharides and a 74-kDa protein with immature, high-mannose N-linked oligosaccharides. Based on these characteristics, we designated the U100 gene products glycoprotein Q (gQ). Only the 80-kDa form of gQ was coimmunoprecipitated with an anti-gH antibody, suggesting that the 80-kDa protein associates with the gH-gL complex in HHV-6-infected cells. Furthermore, the complex was detected in purified virions, suggesting that it may play an important role in viral entry.
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IDENTIFICATION OF HUMAN HERPESVIRUS-6 AS A CAUSAL AGENT FOR EXANTHEM SUBITUM
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