Microbial Copper-binding Siderophores at the Host-Pathogen Interface

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 io...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 2015-07, Vol.290 (31), p.18967-18974
Main Authors: Koh, Eun-Ik, Henderson, Jeffrey P.
Format: Article
Language:English
Subjects:
Animals
Bacterial Infections - immunology
Bacterial Infections - microbiology
Coordination Complexes - chemistry
Coordination Complexes - metabolism
copper
Copper - physiology
Escherichia coli - immunology
Escherichia coli - metabolism
host-pathogen interaction
Host-Pathogen Interactions
Humans
Immunity, Innate
microbial pathogenesis
Minireviews
siderophore
Siderophores - physiology
superoxide dismutase (SOD)
Yersinia - immunology
Yersinia - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.R115.644328