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http://purl.uniprot.org/citations/2849025http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2849025http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2849025http://www.w3.org/2000/01/rdf-schema#comment"Cells infected with herpes simplex virus type 1 (HSV-1), but not HSV-2, express on their surfaces a receptor for the complement component C3b. Receptor activity is markedly enhanced by treatment of the infected cells with neuraminidase. Employing a direct binding assay, consisting of purified HSV glycoproteins immobilized on nitrocellulose and iodinated C3b as a probe, we found that C3b binds directly to gC-1, as well as to gC-2, but not to gB or gD from either serotype. C3b binding was enhanced by treatment of gC-1 or gC-2 with neuraminidase. Endo F or endo H treatment of gC-1 had no effect on C3b binding. However, treatment of gC-2 with these endoglycosidases had a marked negative effect on C3b binding. These results suggest that N-linked oligosaccharides are involved in binding of C3b to gC-2, but not gC-1. Alternatively, removal of N-linked oligosaccharides from gC-2 might adversely affect polypeptide conformation. Glycoprotein C-2 also differs from gC-1 in its effects on the complement cascade. Whereas gC-1 accelerated the decay of the alternative pathway C3 convertase and impaired the efficiency of lysis by the components C5 through C9, gC-2 stabilized the active C3 convertase and had little effect on the late-acting components. The dissimilarity of gC-1 and gC-2 with regard to their effects on the complement cascade may have implications regarding the role of these glycoproteins in confronting the host immune response."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.org/dc/terms/identifier"doi:10.1016/0882-4010(87)90012-x"xsd:string
http://purl.uniprot.org/citations/2849025http://purl.org/dc/terms/identifier"doi:10.1016/0882-4010(87)90012-x"xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Cohen G.H."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Cohen G.H."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Eisenberg R.J."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Eisenberg R.J."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Frank M.M."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Frank M.M."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Friedman H.M."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Friedman H.M."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Fries L.F."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Fries L.F."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Hastings J.C."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Hastings J.C."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Ponce de Leon M."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/author"Ponce de Leon M."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/name"Microb. Pathog."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/name"Microb. Pathog."xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/pages"423-435"xsd:string
http://purl.uniprot.org/citations/2849025http://purl.uniprot.org/core/pages"423-435"xsd:string