The Response of Acinetobacter baumannii to Zinc Starvation

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 growt...

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Bibliographic Details
Published in:Cell host & microbe 2016-06, Vol.19 (6), p.826-836
Main Authors: Nairn, Brittany L., Lonergan, Zachery R., Wang, Jiefei, Braymer, Joseph J., Zhang, Yaofang, Calcutt, M. Wade, Lisher, John P., Gilston, Benjamin A., Chazin, Walter J., de Crécy-Lagard, Valerie, Giedroc, David P., Skaar, Eric P.
Format: Article
Language:English
Subjects:
Acinetobacter baumannii - genetics
Acinetobacter baumannii - growth & development
Acinetobacter baumannii - metabolism
Acinetobacter Infections - microbiology
Animals
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Chlorides - metabolism
Gene Expression Regulation, Bacterial
Genes, Bacterial
GTP Phosphohydrolases - metabolism
Histidine - metabolism
Histidine Ammonia-Lyase - metabolism
Metallochaperones - genetics
Metallochaperones - metabolism
Mice
Mice, Inbred C57BL
Mutation
Zinc - deficiency
Zinc - metabolism
Zinc Compounds - metabolism
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Summary: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. [Display omitted] •A. baumannii responds to Zn starvation by upregulating a Zn metallochaperone ZigA•ZigA is a Zn-binding GTPase that impacts intracellular histidine levels in low Zn•The histidine ammonia-lyase HutH is activated by Zn, potentially obtained from ZigA•Histidine is a labile Zn pool mobilized during low Zn via histidine degradation by HutH Zinc (Zn) is an essential metal that vertebrates sequester from pathogens to protect against infection. Nairn et al. show that the nosocomial opportunistic pathogen A. baumannii’s response to Zn starvation involves both the upregulation of a Zn-binding metallochaperone and by mobilization of a labile histidine-bound Zn pool via histidine degradation.
ISSN:1931-3128
1934-6069
DOI:10.1016/j.chom.2016.05.007