HUMAN PARAINFLUENZA VIRUS TYPE-2 PHOSPHOPROTEIN - MAPPING OF MONOCLONAL-ANTIBODY EPITOPES AND LOCATION OF THE MULTIMERIZATION DOMAIN

The epitopes recognized by 42 monoclonal antibodies directed against t he human parainfluenza virus type 2 (hPIV-2) phosphoprotein (P) were m apped on the primary structure of the P protein by testing their react ivities with deletion mutants. By Western immunoblotting with these mo noclonal antibodies and P protein deletion mutants the region essentia l for P-P interactions was determined. The P protein region encompassi ng amino acids 211-248 was required for proper folding and oligomeriza tion which is mediated by predicted coiled-coils in this region. The o ligomer was shown to be a homotrimer by chemical cross-linking experim ents.