PerR controls Mn‐dependent resistance to oxidative stress inNeisseria gonorrhoeae

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Abstract
Summary: In previous studies it has been established that resistance to superoxide byNeisseria gonorrhoeaeis dependent on the accumulation of Mn(II) ions involving the ABC transporter, MntABC. A mutant strain lacking the periplasmic binding protein component (MntC) of this transport system is hypersensitive to killing by superoxide anion. In this study themntCmutant was found to be more sensitive to H2O2killing than the wild‐type. Analysis of regulation of MntC expression revealed that it was de‐repressed under low Mn(II) conditions. TheN. gonorrhoeae mntABClocus lacks themntRrepressor typically found associated with this locus in other organisms. A search for a candidate regulator ofmntABCexpression revealed a homologue of PerR, a Mn‐dependent peroxide‐responsive regulator found in Gram‐positive organisms. AperRmutant expressed more MntC protein than wild‐type, and expression was independent of Mn(II), consistent with a role for PerR as a repressor ofmntABCexpression. The PerR regulon ofN. gonorrhoeaewas defined by microarray analysis and includes ribosomal proteins, TonB‐dependent receptors and an alcohol dehydrogenase. Both themntCandperRmutants had reduced intracellular survival in a human cervical epithelial cell model.

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