The aminoglycoside resistance-promoting AmgRS envelope stress-responsive two-component system in Pseudomonas aeruginosa is zinc-activated and protects cells from zinc-promoted membrane damage.


Journal

Microbiology (Reading, England)
ISSN: 1465-2080
Titre abrégé: Microbiology (Reading)
Pays: England
ID NLM: 9430468

Informations de publication

Date de publication:
05 2019
Historique:
pubmed: 6 3 2019
medline: 15 1 2020
entrez: 6 3 2019
Statut: ppublish

Résumé

Exposure of wild-type (WT) Pseudomonas aeruginosa PAO1 to ZnCl2 (Zn) yielded a concentration-dependent increase in depolarization of the cytoplasmic membrane (CM), an indication that this metal is membrane-damaging. Consistent with this, Zn activated the AmgRS envelope stress-responsive two-component system (TCS) that was previously shown to be activated by and to protect P. aeruginosa from the membrane-damaging effects of aminoglycoside (AG) antibiotics. A mutant lacking amgR showed enhanced Zn-promoted CM perturbation and was Zn-sensitive, an indication that the TCS protected cells from the CM-damaging effects of this metal. In agreement with this, a mutant carrying an AmgRS-activating amgS mutation was less susceptible to Zn-promoted CM perturbation and more tolerant of elevated levels of Zn than WT. AG activation of AmgRS is known to drive expression of the AG resistance-promoting mexXY multidrug efflux operon, and while Zn similarly induced mexXY expression this was independent of AmgRS and reliant on a second TCS implicated in mexXY regulation, ParRS. MexXY did not, however, contribute to Zn resistance or protection from Zn-promoted CM damage. Despite its activation of AmgRS and induction of mexXY, Zn had a minimal impact on the AG resistance of WT P. aeruginosa although, given that Zn-tolerant AmgRS-activated amgS mutant strains are AG resistant, there is still the prospect of this metal promoting AG resistance development in this organism.

Identifiants

pubmed: 30835196
doi: 10.1099/mic.0.000787
doi:

Substances chimiques

Aminoglycosides 0
Anti-Bacterial Agents 0
Bacterial Proteins 0
Zinc J41CSQ7QDS

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

563-571

Subventions

Organisme : CIHR
Pays : Canada

Auteurs

Keith Poole (K)

Department of Biomedical and Molecular Sciences, Botterell Hall, Queen's University, Kingston, Ontario, K7L 3N6, Canada.

Thomas Hay (T)

Department of Biomedical and Molecular Sciences, Botterell Hall, Queen's University, Kingston, Ontario, K7L 3N6, Canada.

Christie Gilmour (C)

Department of Biomedical and Molecular Sciences, Botterell Hall, Queen's University, Kingston, Ontario, K7L 3N6, Canada.

Michael Fruci (M)

Department of Biomedical and Molecular Sciences, Botterell Hall, Queen's University, Kingston, Ontario, K7L 3N6, Canada.
Present address: London Research and Development Centre, Agriculture and Agri-Food, London, Ontario, Canada.

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Classifications MeSH