Nature Chemical Biology
Nature Chemical Biology
4 years ago

Copper import in Escherichia coli by the yersiniabactin metallophore system

Copper import in Escherichia coli by the yersiniabactin metallophore system
Anne E Robinson, Jeffrey P Henderson, Nilantha Bandara, Buck E Rogers, Eun-Ik Koh
Copper plays a dual role as a nutrient and a toxin during bacterial infections. While uropathogenic Escherichia coli (UPEC) strains can use the copper-binding metallophore yersiniabactin (Ybt) to resist copper toxicity, Ybt also converts bioavailable copper to Cu(II)–Ybt in low-copper conditions. Although E. coli have long been considered to lack a copper import pathway, we observed Ybt-mediated copper import in UPEC using canonical Fe(III)–Ybt transport proteins. UPEC removed copper from Cu(II)–Ybt with subsequent re-export of metal-free Ybt to the extracellular space. Copper released through this process became available to an E. coli cuproenzyme (the amine oxidase TynA), linking this import pathway to a nutrient acquisition function. Ybt-expressing E. coli thus engage in nutritional passivation, a strategy of minimizing a metal ion's toxicity while preserving its nutritional availability. Copper acquisition through this process may contribute to the marked virulence defect of Ybt-transport-deficient UPEC.

Publisher URL: http://dx.doi.org/10.1038/nchembio.2441

DOI: 10.1038/nchembio.2441

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