PerR controls Mn-dependent resistance to oxidative stress in Neisseria gonorrhoeae
Date
2006
Authors
Wu, H.
Seib, K.
Srikhanta, Y.
Kidd, S.
Edwards, J.
Maguire, T.
Grimmond, S.
Apicella, M.
McEwan, A.
Jennings, M.
Editors
Advisors
Journal Title
Journal ISSN
Volume Title
Type:
Journal article
Citation
Molecular Microbiology, 2006; 60(2):401-416
Statement of Responsibility
Hsing-Ju Wu, Kate L. Seib, Yogitha N. Srikhanta, Stephen P. Kidd, Jennifer L. Edwards, Tina L. Maguire, Sean M. Grimmond, Michael A. Apicella, Alastair G. McEwan and Michael P. Jennings
Conference Name
Abstract
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 H2O2 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.