Loading…
Metal selectivity by the virulence-associated yersiniabactin metallophore systemElectronic supplementary information (ESI) available. See DOI: 10.1039/c4mt00341a
Uropathogenic Escherichia coli secrete siderophores during human infections. Although siderophores are classically defined by their ability to bind iron( iii ) ions, the virulence-associated siderophore yersiniabactin was recently found to bind divalent copper ions during urinary tract infections. H...
Saved in:
Main Authors: | , , , , , |
---|---|
Format: | Article |
Language: | English |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Uropathogenic
Escherichia coli
secrete siderophores during human infections. Although siderophores are classically defined by their ability to bind iron(
iii
) ions, the virulence-associated siderophore yersiniabactin was recently found to bind divalent copper ions during urinary tract infections. Here we use a mass spectrometric approach to determine the extent of non-iron(
iii
) metal interactions by yersiniabactin and its TonB-dependent outer membrane importer FyuA. In addition to copper, iron and gallium ions, yersiniabactin was also observed to form stable nickel, cobalt, and chromium ion complexes. In
E. coli
, copper(
ii
) and all other non-iron(
iii
) yersiniabactin complexes were imported by FyuA in a TonB-dependent manner. Among metal-yersiniabactin complexes, copper(
ii
) yersiniabactin is predicted to be structurally distinctive and was the only complex not to competitively inhibit iron(
iii
) yersiniabactin import. These results are consistent with yersiniabactin as part of a metallophore system able to prioritize iron(
iii
) complex uptake in high copper environments.
Metal-yersiniabactin complexes are transported intact through the outer membrane receptor, FyuA, in a TonB-dependent manner in uropathogenic
Escherichia coli
. |
---|---|
ISSN: | 1756-5901 1756-591X |
DOI: | 10.1039/c4mt00341a |