SURFACE-ANTIGEN ANALYSIS OF GROUP-B NEISSERIA-MENINGITIDIS OUTER-MEMBRANE BY MONOCLONAL-ANTIBODIES - IDENTIFICATION OF BACTERICIDAL ANTIBODIES TO CLASS-5 PROTEIN

Twenty-four monoclonal antibodies (mAbs) against group B Neisseria men ingitidis surface antigens were analyzed by immunoenzymatic assays and by a bactericidal test. Two mAbs were specific to polysaccharide B an d one to lipopolysaccharide. The others were directed against outer me mbrane proteins ranging in molecular mass from 25 to 200 kDa. The oute r membrane protein epitopes recognized by the mAbs were not conformati onal and were located on the outer surface of the microorganism. Linea r epitopes on the class 5 protein, exposed on the surface of the membr ane, were able to induce bactericidal antibodies to the homologous str ain. The susceptibility of Neisseria meningitidis to these antibodies was unchanged when this organism was cultivated under conditions of ir on depletion. These results demonstrate that peptides derived from cla ss 5 proteins are potentially important in synthetic peptide or in rec ombinant protein vaccines containing linear bactericidal epitopes.