Analysis of the expression of the putatively virulence-associated neisserial protein RmpM (class 4) in commensal Neisseria and Moraxella catarrhalis strains

Autor: G Troncoso, M.T. Criado, Einar Rosenqvist, Carlos M. Ferreirós, Jan Kolberg, Manuel Veiga, Sandra Sánchez
Rok vydání: 2001
Předmět:
Zdroj: FEMS Microbiology Letters. 199:171-176
ISSN: 1574-6968
0378-1097
DOI: 10.1111/j.1574-6968.2001.tb10669.x
Popis: The RmpM protein has been reported to be present only in pathogenic Neisseria species. In the present study we demonstrate that this protein is also present at least in N. lactamica and N. sicca strains. The N. lactamica protein reacts with a RmpM-specific monoclonal antibody (185,H-8), having a molecular mass ( approximately 31 kDa) slightly lower than that of the meningococcal RmpM, and mouse antibodies from sera against outer membrane vesicles from both N. lactamica and N. sicca strains cross-react with the meningococcal RmpM. PCR and hybridization experiments with a complete rmpM probe agree with the immunodetection experiments. Our results strongly suggest that the meningococcal RmpM should not be considered a virulence marker, and the presence of this protein in the commensal species agrees with its role as a structural protein, proposed for the RmpM, which should be considerably conserved in the Neisseria species.
Databáze: OpenAIRE