Characterization of epitopes on the rabies virus glycoprotein by selection and analysis of escape mutants

Abstract

Rabies virus, a negative sense single-stranded RNA virus, is the type member of the genus Lyssavirus of the Rhabdoviridae . The glycoprotein (G), which projects from the surface of the lyssavirus particle, is the only protein known to be capable of eliciting the production of neutralizing antibodies and knowledge of the antigenic nature of this protein is therefore important. Five different antigenic sites have been mapped on the G protein. In this study, the isolation of mutants resisting antibody neutralization (escape mutants) was attempted by a selection strategy employing three distinct strains of rabies: Evelyn Rokitnicki Abelseth (ERA), Big Brown Bat (BBB), and Silver Haired Bat (SHB). No escape mutants were generated from BBB and SHB but a total of seven independent ERA mutants were recovered using monoclonal antibodies (Mabs) directed against antigenic sites I and IIIa of the glycoprotein. (Abstract shortened by UMI.)