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Microbial Copper-binding Siderophores at the Host-Pathogen Interface.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2015 Jul 31; Vol. 290 (31), pp. 18967-74. Date of Electronic Publication: 2015 Jun 08. - Publication Year :
- 2015
-
Abstract
- 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.<br /> (© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.)
- Subjects :
- Animals
Bacterial Infections immunology
Bacterial Infections microbiology
Coordination Complexes chemistry
Coordination Complexes metabolism
Escherichia coli immunology
Escherichia coli metabolism
Humans
Immunity, Innate
Yersinia immunology
Yersinia metabolism
Copper physiology
Host-Pathogen Interactions
Siderophores physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 290
- Issue :
- 31
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 26055720
- Full Text :
- https://doi.org/10.1074/jbc.R115.644328