1. Pseudomonas aeruginosa T6SS-mediated molybdate transport contributes to bacterial competition during anaerobiosis
- Author
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Tietao Wang, Linxuan Ji, Yuying Han, Jing Wen, Yarong Wang, Haihua Liang, Xiao Du, Qinqin Pu, Min Wu, and Jing Dang
- Subjects
0301 basic medicine ,QH301-705.5 ,Virulence Factors ,medicine.disease_cause ,General Biochemistry, Genetics and Molecular Biology ,03 medical and health sciences ,Mice ,0302 clinical medicine ,Bacterial Proteins ,medicine ,Animals ,Secretion ,Pseudomonas Infections ,Anaerobiosis ,Biology (General) ,Gene ,Type VI secretion system ,Molybdenum ,Metalloproteinase ,Ion Transport ,Microbial Viability ,biology ,Virulence ,Pseudomonas aeruginosa ,Effector ,Chemistry ,Metalloendopeptidases ,Gene Expression Regulation, Bacterial ,Anr regulator ,Type VI Secretion Systems ,biology.organism_classification ,molybdate acquisition ,Survival Analysis ,Cell biology ,Mice, Inbred C57BL ,T6SS ,030104 developmental biology ,anaerobic condition ,Trans-Activators ,Microbial Interactions ,Female ,Bacterial outer membrane ,Carrier Proteins ,030217 neurology & neurosurgery ,Bacteria - Abstract
Summary Type VI secretion system (T6SS) is widely distributed in Gram-negative bacteria and functions as a versatile protein export machinery that translocates effectors into eukaryotic or prokaryotic target cells. Growing evidence indicates that T6SS can deliver several effectors to promote bacterial survival in harmful environments through metal ion acquisition. Here, we report that the Pseudomonas aeruginosa H2-T6SS mediates molybdate (MoO42−) acquisition by secretion of a molybdate-binding protein, ModA. The expression of H2-T6SS genes is activated by the master regulator Anr and anaerobiosis. We also identified a ModA-binding protein, IcmP, an insulin-cleaving metalloproteinase outer membrane protein. The T6SS-ModA-IcmP system provides P. aeruginosa with a growth advantage in bacterial competition under anaerobic conditions and plays an important role in bacterial virulence. Overall, this study clarifies the role of T6SS in secretion of an anion-binding protein, emphasizing the fundamental importance of this bacterium using T6SS-mediated molybdate uptake to adapt to complex environmental conditions.
- Published
- 2020