The siderophore yersiniabactin binds copper to protect pathogens during infection

Kaveri S. Chaturvedi, Chia S. Hung, Jan R. Crowley, Ann E. Stapleton, Jeffrey P. Henderson

Research output: Contribution to journalArticlepeer-review

214 Scopus citations


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.

Original languageEnglish
Pages (from-to)731-736
Number of pages6
JournalNature Chemical Biology
Issue number8
StatePublished - Aug 2012


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