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Cupric yersiniabactin is a virulence-associated superoxide dismutase mimic.


ABSTRACT: Many Gram-negative bacteria interact with extracellular metal ions by expressing one or more siderophore types. Among these, the virulence-associated siderophore yersiniabactin (Ybt) is an avid copper chelator, forming stable cupric (Cu(II)-Ybt) complexes that are detectable in infected patients. Here we show that Ybt-expressing E. coli are protected from intracellular killing within copper-replete phagocytic cells. This survival advantage is highly dependent upon the phagocyte respiratory burst, during which superoxide is generated by the NADPH oxidase complex. Chemical fractionation links this phenotype to a previously unappreciated superoxide dismutase (SOD)-like activity of Cu(II)-Ybt. Unlike previously described synthetic copper-salicylate (Cu(II)-SA) SOD mimics, the salicylate-based natural product Cu(II)-Ybt retains catalytic activity at physiologically plausible protein concentrations. These results reveal a new virulence-associated adaptation based upon spontaneous assembly of a non-protein catalyst.

SUBMITTER: Chaturvedi KS 

PROVIDER: S-EPMC3934373 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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Cupric yersiniabactin is a virulence-associated superoxide dismutase mimic.

Chaturvedi Kaveri S KS   Hung Chia S CS   Giblin Daryl E DE   Urushidani Saki S   Austin Anthony M AM   Dinauer Mary C MC   Henderson Jeffrey P JP  

ACS chemical biology 20131211 2


Many Gram-negative bacteria interact with extracellular metal ions by expressing one or more siderophore types. Among these, the virulence-associated siderophore yersiniabactin (Ybt) is an avid copper chelator, forming stable cupric (Cu(II)-Ybt) complexes that are detectable in infected patients. Here we show that Ybt-expressing E. coli are protected from intracellular killing within copper-replete phagocytic cells. This survival advantage is highly dependent upon the phagocyte respiratory burst  ...[more]

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