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- W4313385846 abstract "Abstract During an inflammatory response in the gut, several commensal bacteria such as E.coli not only survive but also thrive and consequently contribute to the disease pathogenesis. The mechanisms by which such opportunistic pathogens bloom despite the hostile pro-inflammatory milieu of the inflamed gut remain largely unknown. We demonstrated that enterobactin (Ent), a siderophore released by E. coli, is a potent inhibitor of a key bactericidal enzyme of the host innate immune system, myeloperoxidase (MPO). The inhibitory activity is specific as glycosylated Ent (salmochelin) and non-catecholate siderophores such as yersiniabactin and ferrichrome failed to inhibit MPO activity. An E. coli ferrienterobactin permease mutant (ΔfepA) overexpressing Ent, but not 3-dehydroquinate synthase (ΔaroB)/ΔfepA double mutant inhibited MPO activity and exhibited enhanced survival in inflamed guts. This survival advantage was counter-regulated by the host siderophore binding protein, lipocalin 2, which rescued MPO from Ent-mediated inhibition. Spectral analysis revealed 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." @default.
- W4313385846 created "2023-01-06" @default.
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- W4313385846 date "2015-05-01" @default.
- W4313385846 modified "2023-10-18" @default.
- W4313385846 title "Survival advantage of <i>E. coli</i> in the inflamed gut is mechanistically linked to enterobactin-mediated inhibition of myeloperoxidase and regulation by lipocalin 2 (MPF4P.736)" @default.
- W4313385846 doi "https://doi.org/10.4049/jimmunol.194.supp.136.12" @default.
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