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Metalloprotease Vsm Is the Major Determinant of Toxicity for Extracellular Products of Vibrio splendidus
Provedor de dados: 5
Autores: Binesse, J; Delsert, Claude; Saulnier, Denis; Champomier Verges, M; Zagorec, M; Munier Lehmann, H; Mazel, D; Le Roux, F.
Genomic data combined with reverse genetic approaches have contributed to the characterization of major virulence factors of Vibrio species; however, these studies have targeted primarily human pathogens. Here, we investigate virulence factors in the oyster pathogen Vibrio splendidus LGP32 and show that toxicity is correlated to the presence of a metalloprotease and its corresponding vsm gene. Comparative genomics showed that an avirulent strain closely related to LGP32 lacked the metalloprotease. The toxicity of LGP32 metalloprotease was confirmed by exposing mollusk and mouse fibroblastic cell lines to extracellular products (ECPs) of the wild type (wt) and a vsm deletion mutant (Delta vsm mutant). The ECPs of the wt induced a strong cytopathic effect...
Tipo: Text
Ano: 2008
URL: http://archimer.ifremer.fr/doc/2008/publication-4931.pdf