ArticleInfection and immunity2009
A periplasmic thioredoxin-like protein plays a role in defense against oxidative stress in Neisseria gonorrhoeae.
Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Preclinical Evaluation of Novel ConservedVaccines · 2026Article
- Transcriptomic Analysis ofInternational journal of molecular sciences · 2025Article
- Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022Review
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- Comparative Genomics of Clinical Isolates of the Emerging Tick-Borne PathogenMicroorganisms · 2021Article
- Oxidative Stress-Generating Antimicrobials, a Novel Strategy to Overcome Antibacterial Resistance.Antioxidants (Basel, Switzerland) · 2020Review
- Signal Recognition Particle RNA Contributes to Oxidative Stress Response inFrontiers in microbiology · 2020Article
- Article
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Frontiers in microbiology · 2015Review
- Functional and structural characterization of protein disulfide oxidoreductase from Thermus thermophilus HB27.Extremophiles : life under extreme conditions · 2014Article
- Comparison of leaf proteomes of cassava (Manihot esculenta Crantz) cultivar NZ199 diploid and autotetraploid genotypes.PloS one · 2014Article
- Structural and functional characterization of ScsC, a periplasmic thioredoxin-like protein from Salmonella enterica serovar Typhimurium.Antioxidants & redox signaling · 2013Article
- Article
- Fur-mediated global regulatory circuits in pathogenic Neisseria species.Journal of bacteriology · 2012Review
- A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Frontiers in cellular and infection microbiology · 2012Review
- Characterization of DsbD in Neisseria meningitidis.Molecular microbiology · 2011Article
- Resistance of Neisseria gonorrhoeae to neutrophils.Frontiers in microbiology · 2011Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thioredoxin-like proteins of the TlpA/ResE/CcmG subfamily are known to face the periplasm in gram-negative bacteria. Using the tlpA gene of Bradyrhizobium japonicum as a query, we identified a locus (NGO1923) in Neisseria gonorrhoeae that encodes a thioredoxin-like protein (NG_TlpA). Bioinformatics analysis indicated that the predicted NG_TlpA protein contained a cleavable signal peptide at the N terminus, and secondary structure analysis identified a thioredoxin fold with a helical insertion (approximately 25 residues), similar to that found in B. japonicum TlpA but absent in cytoplasmic thioredoxins. Biochemical characterization of a recombinant form of NG_TlpA revealed a standard redox potential (E0') of -206 mV. This property and the observation that the oxidized form of the protein exhibited greater thermal stability than the reduced species indicated that NG_TlpA is a reducing thioredoxin and not an oxidizing thiol-disulfide oxidoreductase like DsbA. The thioredoxin activity of NG_TlpA was confirmed in an insulin disulfide reduction assay. A tlpA mutant of N. gonorrhoeae strain 1291 was found to be highly sensitive to oxidative killing by paraquat and hydrogen peroxide, indicating an antioxidant role for the NG_TlpA in this bacterium. The tlpA mutant also exhibited reduced intracellular survival in human primary cervical epithelial cells.
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