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Type: Journal article
Title: Thioredoxin reductase is essential for protection of neisseria gonorrhoeae against killing by nitric oxide and for bacterial growth during interaction with cervical epithelial cells
Author: Potter, A.
Kidd, S.
Edwards, J.
Falsetta, M.
Apicella, M.
Jennings, M.
McEwan, A.
Citation: Journal of Infectious Diseases, 2009; 199(2):227-235
Publisher: University of Chicago Press
Issue Date: 2009
ISSN: 0022-1899
Statement of
Adam J. Potter, Stephen P. Kidd, Jennifer L. Edwards, Megan L. Falsetta, Michael A. Apicella, Michael P. Jennings and Alastair G. McEwan
Abstract: In Neisseria gonorrhoeae, the MerR family transcription factor NmlR activates 3 operons in response to disulfide stress. In the present study, we show that trxB, a monocistronic operon under the control of NmlR, encodes a functional thioredoxin reductase. It is shown that neisserial TrxB has biochemical properties similar to those of its homologue from Escherichia coli. Analysis of a trxB mutant of N. gonorrhoeae showed that it was more sensitive to disulfide stress and to stress induced by organic hydroperoxides, superoxide, and nitric oxide than wild‐type gonococcus. TrxB was found to be essential for the microaerobic induction of aniA and norB, the genes encoding nitrite reductase and nitric oxide reductase, respectively. The importance of TrxB during natural infection was demonstrated by the fact that the survival of gonococci within human cervical epithelial cells, as well as biofilm formation on these cells, was greatly reduced for a trxB mutant compared with a wild‐type strain.
Keywords: Cervix Uteri
Cells, Cultured
Epithelial Cells
Neisseria gonorrhoeae
Nitric Oxide
Nitrite Reductases
Microbial Sensitivity Tests
Base Sequence
Molecular Sequence Data
Thioredoxin-Disulfide Reductase
DOI: 10.1086/595737
Appears in Collections:Aurora harvest
Molecular and Biomedical Science publications

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