Surface antigen analysis of group B Neisseria meningitidis outer membrane by monoclonal antibodies: Identification of bactericidal antibodies to class 5 protein |
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Authors: | Maria das Graças M. Danelli Nádia M. Batoreu Maria Diana Lacerda Cristiane R. B. Ferreira Joana Darc Cardoso José M. Peralta Carl E. Frasch |
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Affiliation: | (1) Departamento de Desenvolvimento Tecnológico, Instituto de Tecnologia em Immunobiológicos (Bio-Manguinhos), Fundação Oswaldo Cruz, Av. Brasil 4365, 21045-900 Rio de Janeiro, RJ, Brazil;(2) Instituto de Microbiologia, Universidade Federal do Rio de Janeiro, 21941 Rio de Janeiro, RJ, Brazil;(3) Center for Biologics Evaluation and Research, Food and Drug Administration, 20892 Bethesda, MD, USA |
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Abstract: | Twenty-four monoclonal antibodies (mAbs) against group B Neisseria meningitidis surface antigens were analyzed by immunoenzymatic assays and by a bactericidal test. Two mAbs were specific to polysaccharide B and one to lipopolysaccharide. The others were directed against outer membrane proteins ranging in molecular mass from 25 to 200 kDa. The outer membrane protein epitopes recognized by the mAbs were not conformational and were located on the outer surface of the microorganism. Linear epitopes on the class 5 protein, exposed on the surface of the membrane, were able to induce bactericidal antibodies to the homologous strain. The susceptibility of Neisseria meningitidis to these antibodies was unchanged when this organism was cultivated under conditions of iron depletion. These results demonstrate that peptides derived from class 5 proteins are potentially important in synthetic peptide or in recombinant protein vaccines containing linear bactericidal epitopes. |
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