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Cell Host Microbe. 2016 Jun 8;19(6):826-36. doi: 10.1016/j.chom.2016.05.007.

The Response of Acinetobacter baumannii to Zinc Starvation.

Author information

1
Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
2
Department of Chemistry, Indiana University, Bloomington, IN 47405, USA.
3
Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
4
Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
5
Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA; Department of Chemistry, Vanderbilt University, Nashville, TN 37232, USA.
6
Department of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611, USA.
7
Department of Chemistry, Indiana University, Bloomington, IN 47405, USA. Electronic address: giedroc@indiana.edu.
8
Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA; Tennessee Valley Healthcare Systems, US Department of Veterans Affairs, Nashville, TN 37232, USA. Electronic address: eric.skaar@vanderbilt.edu.

Abstract

Zinc (Zn) is an essential metal that vertebrates sequester from pathogens to protect against infection. Investigating the opportunistic pathogen Acinetobacter baumannii's response to Zn starvation, we identified a putative Zn metallochaperone, ZigA, which binds Zn and is required for bacterial growth under Zn-limiting conditions and for disseminated infection in mice. ZigA is encoded adjacent to the histidine (His) utilization (Hut) system. The His ammonia-lyase HutH binds Zn very tightly only in the presence of high His and makes Zn bioavailable through His catabolism. The released Zn enables A. baumannii to combat host-imposed Zn starvation. These results demonstrate that A. baumannii employs several mechanisms to ensure bioavailability of Zn during infection, with ZigA functioning predominately during Zn starvation, but HutH operating in both Zn-deplete and -replete conditions to mobilize a labile His-Zn pool.

PMID:
27281572
PMCID:
PMC4901392
DOI:
10.1016/j.chom.2016.05.007
[Indexed for MEDLINE]
Free PMC Article

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