MAPPING OF MONOCLONAL-ANTIBODY EPITOPES OF THE RABIES VIRUS P-PROTEIN

Thirty-six monoclonal antibodies (MAbs) specific for the rabies virus P phosphoprotein were obtained from mice immunized with recombinant P (PV strain) produced in E. coli. All MAbs reacted against the correspo nding rabies virus protein by ELISA and by Western blot analysis and r evealed the presence of cytoplasmic inclusions in rabies virus infecte d cells. The epitopes of seven MAbs were mapped by testing their react ivity with protein fragments expressed from deletion mutants in transf ected cells. Western blotting, immunoprecipitation and immunofluoresce nce assays were performed. These MAbs recognized epitopes in different domains of the P protein: 60% were directed against a region lying be tween residues 83-172 suggesting a major antigenic determinant of the rabies virus P protein in this region. Most of the antigenic sites app eared to be composed of linear epitopes. These MAbs will be useful as tools to dissect structural and functional properties of the rabies vi rus P protein.