title: Microbial Copper-binding Siderophores at the Host-Pathogen Interface.
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.
authors.affiliation: From the Center for Women's Infectious Diseases Research, Division of Infectious Diseases, and Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
authors.forename: Eun-Ik
authors.initials: EI
authors.lastname: Koh
authors.affiliation: From the Center for Women's Infectious Diseases Research, Division of Infectious Diseases, and Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110 jhenderson@DOM.wustl.edu.
authors.forename: Jeffrey P
authors.initials: JP
authors.lastname: Henderson
mesh_terms: D000818:Animals; D001424:Bacterial Infections / Q000276:immunology / Q000382:microbiology; D056831:Coordination Complexes / Q000737:chemistry / Q000378:metabolism; D003300:Copper / Q000502:physiology*; D004926:Escherichia coli / Q000276:immunology / Q000378:metabolism; D054884:Host-Pathogen Interactions; D006801:Humans; D007113:Immunity, Innate; D017262:Siderophores / Q000502:physiology*; D015007:Yersinia / Q000276:immunology / Q000378:metabolism
chemical_list: D056831:Coordination Complexes; D017262:Siderophores; D003300:Copper
keywords: copper; host-pathogen interaction; microbial pathogenesis; siderophore; superoxide dismutase (SOD)