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• W1988022440 abstract "Summary In previous studies it has been established that resistance to superoxide by Neisseria gonorrhoeae is 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 the mntC mutant was found to be more sensitive to H 2 O 2 killing than the wild‐type. Analysis of regulation of MntC expression revealed that it was de‐repressed under low Mn(II) conditions. The N. gonorrhoeae mntABC locus lacks the mntR repressor typically found associated with this locus in other organisms. A search for a candidate regulator of mntABC expression revealed a homologue of PerR, a Mn‐dependent peroxide‐responsive regulator found in Gram‐positive organisms. A perR mutant expressed more MntC protein than wild‐type, and expression was independent of Mn(II), consistent with a role for PerR as a repressor of mntABC expression. The PerR regulon of N. gonorrhoeae was defined by microarray analysis and includes ribosomal proteins, TonB‐dependent receptors and an alcohol dehydrogenase. Both the mntC and perR mutants had reduced intracellular survival in a human cervical epithelial cell model." @default.
• W1988022440 created "2016-06-24" @default.
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• W1988022440 date "2006-03-03" @default.
• W1988022440 modified "2023-09-27" @default.
• W1988022440 title "PerR controls Mn-dependent resistance to oxidative stress in Neisseria gonorrhoeae" @default.
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• W1988022440 doi "https://doi.org/10.1111/j.1365-2958.2006.05079.x" @default.
• W1988022440 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16573689" @default.
• W1988022440 hasPublicationYear "2006" @default.
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