期刊
NATURE CHEMICAL BIOLOGY
卷 8, 期 8, 页码 731-736出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1020
关键词
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资金
- Burroughs-Wellcome Fund
- US National Institutes of Health [K12 HD001459-09, AI 07172-24, P30 HL101263-01, P50 DK64540, U01 DK082315, UL1 RR024992]
- [P41-RR00954]
- [8-P41 GM103422-35]
- [P60-DK20579]
- [P30-DK56341]
Bacterial pathogens secrete chemically diverse iron chelators called siderophores, which may exert additional distinctive functions in vivo. Among these, uropathogenic Escherichia coli often coexpress the virulence-associated siderophore yersiniabactin (Ybt) with catecholate siderophores. Here we used a new MS screening approach to reveal that Ybt is also a physiologically favorable Cu(II) ligand. Direct MS detection of the resulting Cu(II)-Ybt complex in mice and humans with E. coli urinary tract infections demonstrates copper binding to be a physiologically relevant in vivo interaction during infection. Ybt expression corresponded to higher copper resistance among human urinary tract isolates, suggesting a protective role for this interaction. Chemical and genetic characterization showed that Ybt helps bacteria resist copper toxicity by sequestering host-derived Cu(II) and preventing its catechol-mediated reduction to Cu(I). Together, these studies reveal a new virulence-associated function for Ybt that is distinct from iron binding.
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