Antigenicity, cross-reactivity and surface exposure of the Neisseria meningitidis 37 kDa protein (Fbp)
Autor: | Carlos M. Ferreirós, M. Pintor, L. Ferrón, C. Agra, M.T. Criado, José Antonio Caride Gómez, N. B. L. Powell |
---|---|
Rok vydání: | 1996 |
Předmět: |
Antigenicity
Blotting Western Enzyme-Linked Immunosorbent Assay Cross Reactions Neisseria meningitidis medicine.disease_cause Cross-reactivity Microbiology Mice Antigen Bacterial Proteins Iron-Binding Proteins medicine Animals Humans Microscopy Immunoelectron Antigens Bacterial Mice Inbred BALB C General Veterinary General Immunology and Microbiology biology Immunogenicity Public Health Environmental and Occupational Health biology.organism_classification Antibodies Bacterial Infectious Diseases Polyclonal antibodies Periplasmic Binding Proteins biology.protein Molecular Medicine Neisseriaceae Antibody Bacterial Outer Membrane Proteins |
Zdroj: | Vaccine. 14(14) |
ISSN: | 0264-410X |
Popis: | The 37 kDa iron-repressible protein, Fbp, was purified from two Neisseria meningitidis strains by metal-affinity chromatography and used to obtain mouse monospecific polyclonal immune sera. Dot-blot, immunoblotting and whole cell ELISA results demonstrate that the Fbp is present in all 16 N. meningitidis and four commensal Neisseria species tested, is highly antigenic in mouse when injected in pure form, and shows intra- and inter-species antigenic homogeneity, anti-Fbp antibodies being fully cross-reactive using the techniques mentioned. We also found that Fbp molecules (or parts of them) are surface exposed, in disagreement with the proposed exclusively periplasmic localization, although anti-Fbp antibodies seem unable to block iron uptake or to induce complement-mediated killing of the meningococci. Taken along with the high immunogenicity of the purified protein and the complete cross-reactivity of the antibodies elicited, this suggests that the protective effect of the purified Fbp must be further studied to evaluate its inclusion in future vaccine trials. |
Databáze: | OpenAIRE |
Externí odkaz: |