Monoclonal antibodies (Mabs) were produced against outer-membrane proteins (OMPs) of type b. The clones were screened by ELISA with outer-membrane preparations of type b and untypable strains as coating antigens. Antibodies directed against the proteins of mol. wt (10) 43, 37 and 13 were identified by immunoblotting of SDS-PAGE patterns of OMPs. Proteolytic enzyme treatments of the OMPs resulted in reduction of Mab reactivity as measured by ELISA. Furthermore, the absence of reactivity of Mab Hb-2 with a preparation of lipopolysaccharide confirmed the protein nature of its corresponding epitope. Binding assays with live bacteria showed that Hb-2 reacted with a cell surface-exposed antigenic determinant. Mab Hb-2 was bactericidal in the presence of complement. The characterisation of Hb-2 (IgG) by Western immunoblotting analysis revealed that it was directed against the 37 × 10-mol. wt OMP. In a dot-enzyme immunoassay, Hb-2 reacted specifically with 326 strains of type b. It did not cross-react with the other serotypes or untypable strains of or with other bacterial species. This is the first report of a monoclonal antibody identifying a serotype—specific surface-exposed OMP of type b.


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