The RND protein is involved in the vulnibactin export system in Vibrio vulnificus M2799 |
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| Affiliation: | 1. Department of Microbiology, Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan;2. Laboratory of Hygienic Chemistry, College of Pharmaceutical Sciences, Matsuyama University, 4-2 Bunkyo-cho, Matsuyama, Ehime 790-8578, Japan;3. Department of Analytical Chemistry, Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan;1. Institut Pasteur, Unité Récepteurs-Canaux, CNRS-UMR 3571, 25, rue du Dr. Roux, F-75015 Paris, France;2. Department of Biochemistry, Nicolaus Copernicus University, Torun, Poland;3. Institu Pasteur, Plate-Forme de Biophysique des Macromolecules et de leurs Interactions, 75015 Paris, France;1. Institute of Molecular Pathology, Faculty of Military Health Sciences (FMHS), University of Defense (UO), Trebesska 1575, 500 01 Hradec Kralove, Czech Republic;2. Centre of Advanced Studies, FMHS, UO, Hradec Kralove, Czech Republic;3. Department of Radiobiology, FMHS, UO, Hradec Kralove, Czech Republic;1. State Key Laboratory of Bioreactor Engineering, Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism, East China University of Science and Technology, Shanghai 200237, China;2. Southern Marine Science and Engineering Guangdong Laboratory (Zhuhai), Zhuhai 519000, China;3. Shanghai Engineering Research Center of Maricultured Animal Vaccines, Shanghai 200237, China |
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| Abstract: | Vibrio vulnificus, an opportunistic marine bacterium that causes a serious, often fatal, infection in humans, requires iron for its pathogenesis. This bacterium exports vulnibactin for iron acquisition from the environment. The mechanisms of vulnibactin biosynthesis and ferric-vulnibactin uptake systems have recently been reported, while the vulnibactin export system has not been reported. Mutant growth under low-iron concentration conditions and a bioassay of the culture supernatant indicate that the VV1_0612 protein plays a crucial role in the vulnibactin secretion as a component of the resistance-nodulation-division (RND)-type efflux system in V. vulnificus M2799. To identify which RND protein(s) together with VV1_0612 TolC constituted the RND efflux system for vulnibactin secretion, deletion mutants of 11 RND protein-encoding genes were constructed. The growth inhibition of a multiple mutant (Δ11) of the RND protein-encoding genes was observed 6 h after the beginning of the culture. Furthermore, ΔVV1_1681 exhibited a growth curve that was similar to that of Δ11, while the multiple mutant except ΔVV1_1681 showed the same growth as the wild-type strain. These results indicate that the VV1_1681 protein is involved in the vulnibactin export system of V. vulnificus M2799. This is the first genetic evidence that vulnibactin is secreted through the RND-type efflux systems in V. vulnificus. |
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