Minireviews
Microbial Copper-binding Siderophores at the Host-Pathogen Interface*

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Numerous pathogenic microorganisms secrete small molecule chelators called siderophores defined by their ability to bind extracellular ferric iron, making it bioavailable to microbes. Recently, a siderophore produced by uropathogenic Escherichia coli, yersiniabactin, was found to also bind copper ions during human infections. The ability of yersiniabactin to protect E. coli from copper toxicity and redox-based phagocyte defenses distinguishes it from other E. coli siderophores. Here we compare yersiniabactin to other extracellular copper-binding molecules and review how copper-binding siderophores may confer virulence-associated gains of function during infection pathogenesis.

copper
host-pathogen interaction
microbial pathogenesis
siderophore
superoxide dismutase (SOD)

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*

This work was supported by a Career Award for Medical Scientists from the Burroughs Wellcome Fund and National Institutes of Health Grant R01DK099534 (to J. P. H.) through the NIDDK. This is the fourth article in the Thematic Minireview series “Metals at the Host-Pathogen Interface.” The authors declare that they have no conflicts of interest with the contents of this article.