SURFACE-ANTIGEN ANALYSIS OF GROUP-B NEISSERIA-MENINGITIDIS OUTER-MEMBRANE BY MONOCLONAL-ANTIBODIES - IDENTIFICATION OF BACTERICIDAL ANTIBODIES TO CLASS-5 PROTEIN
Mdm. Danelli et al., SURFACE-ANTIGEN ANALYSIS OF GROUP-B NEISSERIA-MENINGITIDIS OUTER-MEMBRANE BY MONOCLONAL-ANTIBODIES - IDENTIFICATION OF BACTERICIDAL ANTIBODIES TO CLASS-5 PROTEIN, Current microbiology, 31(3), 1995, pp. 146-151
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.