Antigenic structure of the herpes simplex virus type 1 glycoprotein C: demonstration of a linear epitope situated in an environment of highly conformation-dependent epitopes.
A 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.
Sjöblom
I
I
Department of Clinical Virology, University of Gothenburg, Sweden.
Glorioso
J C
JC
Sjögren-Jansson
E
E
Olofsson
S
S
D000911:Antibodies, Monoclonal / Q000302:isolation & purification; D000939:Epitopes / Q000032:analysis*; D006023:Glycoproteins / Q000276:immunology*; D018139:Simplexvirus / Q000276:immunology*; D014415:Tunicamycin / Q000494:pharmacology; D014759:Viral Envelope Proteins / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000939:Epitopes; D006023:Glycoproteins; D014759:Viral Envelope Proteins; C038535:glycoprotein gC, herpes simplex virus type 1; D014415:Tunicamycin