The PerR-regulated P1B-4 type ATPase (PmtA) acts as a ferrous iron efflux pump in Streptococcus pyogenes

Turner, Andrew G., Ong, Cheryl-lynn Y., Djoko, Karrera Y., West, Nicholas P., Davies, Mark R., McEwan, Alastair G. and Walker, Mark J. (2017) The PerR-regulated P1B-4 type ATPase (PmtA) acts as a ferrous iron efflux pump in Streptococcus pyogenes. Infection and Immunity, 85 6: e00140-17.1-e00140-17.13. doi:10.1128/IAI.00140-17

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Author Turner, Andrew G.
Ong, Cheryl-lynn Y.
Djoko, Karrera Y.
West, Nicholas P.
Davies, Mark R.
McEwan, Alastair G.
Walker, Mark J.
Title The PerR-regulated P1B-4 type ATPase (PmtA) acts as a ferrous iron efflux pump in Streptococcus pyogenes
Formatted title
The PerR-regulated P1B-4 type ATPase (PmtA) acts as a ferrous iron efflux pump in Streptococcus pyogenes
Journal name Infection and Immunity   Check publisher's open access policy
ISSN 1098-5522
0019-9567
Publication date 2017-04-03
Year available 2017
Sub-type Article (original research)
DOI 10.1128/IAI.00140-17
Open Access Status DOI
Volume 85
Issue 6
Start page e00140-17.1
End page e00140-17.13
Total pages 13
Place of publication Washington DC, United States
Publisher American Society for Microbiology
Collection year 2018
Language eng
Formatted abstract
Streptococcus pyogenes (group A Streptococcus; GAS) is an obligate human pathogen responsible for a broad spectrum of human disease. GAS has a requirement for metal homeostasis within the human host and as such, tightly modulates metal uptake and efflux during infection. Metal acquisition systems are required to combat metal sequestration by the host, while metal efflux systems are essential to protect against metal overload poisoning. Here, we investigated the function of PmtA (PerR-regulated metal transporter A), a P1B-4 type ATPase efflux pump, in the invasive GAS M1T1 strain 5448. We reveal that PmtA functions as a ferrous iron [Fe(II)] efflux system. In the presence of high Fe(II) concentrations, the 5448ΔpmtA deletion mutant exhibited diminished growth and accumulated 5-fold higher intracellular Fe(II) compared to the wild-type and complemented mutant. The 5448ΔpmtA deletion mutant also showed enhanced susceptibility to killing by the Fe-dependent antibiotic, streptonigrin, as well as increased sensitivity to hydrogen peroxide and superoxide. We suggest that the PerR-mediated control of Fe(II) efflux by PmtA is important for bacterial defense against oxidative stress. PmtA represents an exemplar for a Fe(II) efflux system in a host-adapted Gram-positive bacterial pathogen.
Keyword Streptococcus pyogenes
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
 
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Created: Fri, 07 Apr 2017, 13:54:55 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences