LINEAR AND CONFORMATION-DEPENDENT ANTIGENIC SITES ON THE NUCLEOPROTEIN OF RABIES VIRUS

A set of 29 monoclonal antibodies (MAbs) specific for the rabies virus nucleoprotein (N protein) was prepared and used to analyze the topogr aphy of antigenic sites. At least four partially overlapping antigenic sites were delineated on the N protein of rabies virus by competitive binding assays. Indirect immunofluorescent antibody tests using MAbs with a series of rabies and rabies-related viruses showed that epitope s shared by various fixed and street strains of rabies virus were main ly localized at antigenic sites II and III, while epitopes representin g the genus-specific antigen of Lyssavirus were widely presented at si tes I, III and IV. All but one of seven MAbs specific for antigenic si tes I, IV and bridge site (I and II) reacted with the antigen that had been denatured by sodium dodecyl sulfate or 2-mercaptoethanol, as wel l as with the denatured N protein in Western blotting assays. However, none of the MAbs against antigenic sites II and III reacted with the denatured antigen. These data indicate that antigenic sites I and IV, and sites II and III on the N protein of rabies virus are composed of linear and conformation-dependent epitopes, respectively.