期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 293, 期 39, 页码 14953-14961出版社
ELSEVIER
DOI: 10.1074/jbc.RA118.004483
关键词
siderophore; nickel; metal homeostasis; metalloenzyme; transport metal; metallophore; nutritional immunity; nutritional passivation; uropathogen
资金
- NIDDK, National Institutes of Health [R01DK099534, R01DK111930]
- Mr. and Mrs. Spencer T. Olin Fellowship for Women in Graduate Study
Invasive Gram-negative bacteria often express multiple virulence-associated metal ion chelators to combat host-mediated metal deficiencies. Escherichia coli, Klebsiella, and Yersinia pestis isolates encoding the Yersinia high pathogenicity island (HPI) secrete yersiniabactin (Ybt), a metallophore originally shown to chelate iron ions during infection. However, our recent demonstration that Ybt also scavenges copper ions during infection led us to question whether it might be capable of retrieving other metals as well. Here, we find that uropathogenic E. coli also use Ybt to bind extracellular nickel ions. Using quantitative MS, we show that the canonical metal-Ybt import pathway internalizes the resulting Ni-Ybt complexes, extracts the nickel, and releases metal-free Ybt back to the extracellular space. We find that E. coli and Klebsiella direct the nickel liberated from this pathway to intracellular nickel enzymes. Thus, Ybt may provide access to nickel that is inaccessible to the conserved NikABCDE permease system. Nickel should be considered alongside iron and copper as a plausible substrate for Ybt-mediated metal import by enterobacteria during human infections.
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