"Locus" NMB0035 codes for a 47-kDa surface-accessible conserved antigen in "Neisseria"
- Jesús Andrés Arenas Busto
- Ana Abel Souto
- Sandra Sánchez Poza
- Belén Alcalá Galicia
- María Teresa Criado Álvarez
- Carlos M. Ferreirós Domínguez
ISSN: 1618-1905
Year of publication: 2006
Volume: 9
Issue: 4
Pages: 273-280
Type: Article
More publications in: International microbiology: official journal of the Spanish Society for Microbiology
Abstract
A47 kDa neisserial outer-membrane antigenic protein (P47) was purified to homogeneity and used to prepare polyclonal anti-P47 antisera. Protein P47 was identified by MALDI-TOF fingerprinting analysis as the hypothetical lipoprotein NMB0035. Two-dimensional diagonal SDS-PAGE results suggested that, contrary to previous findings, P47 is not strongly associated with other proteins in membrane complexes. Western blotting with the polyclonal monospecific serum showed that linear P47 epitopes were expressed in similar amounts in the 27 Neisseria meningitidis strains tested and, to a lesser extent, in commensal Neisseria, particularly N. lactamica. However, dot-blotting assays with the same serum demonstrated binding variability between meningococcal strains, indicating differences in surface accessibility or steric hindrance by other surface structures. Specific anti-P47 antibodies were bactericidal against the homologous strain but had variable activity against heterologous strains, consistent with the results from dot-blotting experiments. An in-depth study of P47 is necessary to evaluate its potential as a candidate for new vaccine designs.