Interplay between enterobactin, myeloperoxidase and lipocalin 2 regulates E. coli survival in the inflamed gut

Vishal Singh, Beng San Yeoh, Xia Xiao, Manish Kumar, Michael Bachman, Niels Borregaard, Bina Joe and Matam Vijay-Kumar ()
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Vishal Singh: Pennsylvania State University
Beng San Yeoh: Pennsylvania State University
Xia Xiao: Pennsylvania State University
Manish Kumar: Pennsylvania State University
Michael Bachman: University of Michigan
Niels Borregaard: The Granulocyte Research Laboratory, National University Hospital, University of Copenhagen
Bina Joe: Center for Hypertension and Personalized Medicine, The University of Toledo College of Medicine and Life Sciences
Matam Vijay-Kumar: Pennsylvania State University

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: Abstract During an inflammatory response in the gut, some commensal bacteria such as E. coli can thrive and contribute to disease. Here we demonstrate that enterobactin (Ent), a catecholate siderophore released by E. coli, is a potent inhibitor of myeloperoxidase (MPO), a bactericidal enzyme of the host. Glycosylated Ent (salmochelin) and non-catecholate siderophores (yersiniabactin and ferrichrome) fail to inhibit MPO activity. An E. coli mutant (ΔfepA) that overproduces Ent, but not an Ent-deficient double mutant (ΔaroB/ΔfepA), inhibits MPO activity and exhibits enhanced survival in inflamed guts. This survival advantage is counter-regulated by lipocalin 2, a siderophore-binding host protein, which rescues MPO from Ent-mediated inhibition. Spectral analysis reveals that Ent interferes with compound I [oxoiron, Fe(IV)=O] and reverts the enzyme back to its native ferric [Fe(III)] state. These findings define a fundamental mechanism by which E. coli surpasses the host innate immune responses during inflammatory gut diseases and gains a distinct survival advantage.

Date: 2015
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DOI: 10.1038/ncomms8113

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