The Response of Acinetobacter baumannii to Zinc Starvation.

Nairn BL, Lonergan ZR, Wang J, Braymer JJ, Zhang Y, Calcutt MW, Lisher JP, Gilston BA, Chazin WJ, de Crécy-Lagard V, Giedroc DP, Skaar EP
Cell Host Microbe. 2016 19 (6): 826-36

PMID: 27281572 · PMCID: PMC4901392 · DOI:10.1016/j.chom.2016.05.007

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.

Copyright © 2016 Elsevier Inc. All rights reserved.

MeSH Terms (16)

Acinetobacter baumannii Acinetobacter Infections Animals Bacterial Proteins Chlorides Gene Expression Regulation, Bacterial Genes, Bacterial GTP Phosphohydrolases Histidine Histidine Ammonia-Lyase Metallochaperones Mice Mice, Inbred C57BL Mutation Zinc Zinc Compounds

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