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pubmed-article:1373286pubmed:abstractTextA continuous epitope, situated within or in close proximity to antigenic site II of the herpes simplex virus type 1-specified glycoprotein C (gC-1), was identified. The continuous linear nature of the epitope, defined by a monoclonal antibody C2H12, was established by three independent lines of evidence: (i) The epitope was detectable by immunoblot under denaturing and reducing conditions. (ii) The epitope was detectable by RIPA of extracts from TM-treated HSV-infected cells, despite the malfolding caused by this treatment. (iii) The epitope was detected in an approximately 5,000-dalton papain fragment of gC-1. A mapping analysis, primarily based on use of mutant virus, expressing truncated gC-1 molecules, suggested that the mapping position of the epitope was delimited by amino acids 120 and 230. Other epitopes of this region of gC-1 are highly conformation-dependent, and the existence of a linear epitope, accessible on native gC-1, may facilitate the elucidation of the functional anatomy of gC-1.lld:pubmed
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pubmed-article:1373286pubmed:pagination229-36lld:pubmed
pubmed-article:1373286pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:1373286pubmed:articleTitleAntigenic structure of the herpes simplex virus type 1 glycoprotein C: demonstration of a linear epitope situated in an environment of highly conformation-dependent epitopes.lld:pubmed
pubmed-article:1373286pubmed:affiliationDepartment of Clinical Virology, University of Gothenburg, Sweden.lld:pubmed
pubmed-article:1373286pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1373286pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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