1. An extracellular serine protease produced by Vibrio vulnificus NCIMB 2137, a metalloprotease-gene negative strain isolated from a diseased eel
- Author
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Jiyou Wang, Yoko Maehara, Keizo Katoh, Shin Ichi Miyoshi, Tamaki Mizuno, and Mitsutoshi Senoh
- Subjects
DNA, Bacterial ,Physiology ,Operon ,medicine.medical_treatment ,Molecular Sequence Data ,Vibrio vulnificus ,Chemical Fractionation ,Applied Microbiology and Biotechnology ,Virulence factor ,Microbiology ,Metalloprotease ,medicine ,Extracellular ,Animals ,Purification ,Serine protease ,Metalloproteinase ,Eels ,Protease ,biology ,Sequence Analysis, DNA ,General Medicine ,Chromatography, Ion Exchange ,biology.organism_classification ,Molecular biology ,Polymerase chain reaction ,Interspersed Repetitive Sequences ,Genes, Bacterial ,Vibrio Infections ,Chromatography, Gel ,biology.protein ,Serine Proteases ,Bacteria ,Biotechnology - Abstract
Vibrio vulnificus is a ubiquitous estuarine microorganism but causes fatal systemic infections in immunocompromised humans, cultured eels or shrimps. An extracellular metalloprotease VVP/VvpE has been reported to be a potential virulence factor of the bacterium; however, a few strains isolated from a diseased eel or shrimp were recently found to produce a serine protease termed VvsA, but not VVP/VvpE. In the present study, we found that these strains had lost the 80 kb genomic region including the gene encoding VVP/VvpE. We also purified VvsA from the culture supernatant through ammonium sulfate fractionation, gel filtration and ion-exchange column chromatography, and the enzyme was demonstrated to be a chymotrypsin-like protease, as well as those from some vibrios. The gene vvsA was shown to constitute an operon with a downstream gene vvsB, and several Vibrio species were found to have orthologues of vvsAB. These findings indicate that the genes vvp/vvpE and vvsAB might be mobile genetic elements.
- Published
- 2011
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