{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["74(23)"],"submitter":["Binesse J"],"pubmed_abstract":["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 (Deltavsm mutant). The ECPs of the wt induced a strong cytopathic effect whose severity was cell type dependen"],"journal":["Applied and environmental microbiology"],"pagination":["7108-17"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2592927"],"repository":["biostudies-literature"],"pubmed_title":["Metalloprotease vsm is the major determinant of toxicity for extracellular products of Vibrio splendidus."],"pmcid":["PMC2592927"],"pubmed_authors":["Binesse J","Le Roux F","Delsert C","Saulnier D","Champomier-Verges MC","Zagorec M","Munier-Lehmann H","Mazel D"],"additional_accession":[]},"is_claimable":false,"name":"Metalloprotease vsm is the major determinant of toxicity for extracellular products of Vibrio splendidus.","description":"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 (Deltavsm mutant). The ECPs of the wt induced a strong cytopathic effect whose severity was cell type dependen","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Dec","modification":"2026-04-30T20:10:33.41Z","creation":"2019-03-27T00:19:36Z"},"accession":"S-EPMC2592927","cross_references":{"pubmed":["18836018"],"doi":["10.1128/AEM.01261-08","10.1128/aem.01261-08"]}}