ArticleCell reports2016
Antioxidant Defense by Thioredoxin Can Occur Independently of Canonical Thiol-Disulfide Oxidoreductase Enzymatic Activity.
Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 33 citations in OpenAlex.
- Antioxidant potential and genomic adaptation ofFrontiers in microbiology · 2026Article
- Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin.Nature communications · 2024Article
- Exploring Immune Redox Modulation in Bacterial Infections: Insights into Thioredoxin-Mediated Interactions and Implications for Understanding Host-Pathogen Dynamics.Antioxidants (Basel, Switzerland) · 2024Review
- The methylglyoxal pathway is a sink for glutathione in Salmonella experiencing oxidative stress.PLoS pathogens · 2023Article
- Gre factors help Salmonella adapt to oxidative stress by improving transcription elongation and fidelity of metabolic genes.PLoS biology · 2023Article
- Promiscuity of response regulators for thioredoxin steers bacterial virulence.Nature communications · 2022Article
- Manganese Utilization inFrontiers in cell and developmental biology · 2022Review
- Antibiotic resistome of Salmonella typhi: molecular determinants for the emergence of drug resistance.Frontiers of medicine · 2021Review
- DksA-DnaJ redox interactions provide a signal for the activation of bacterial RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A straightforward and convenient synthesis of functionalized allyl thiosulfonates and allyl disulfanes.RSC advances · 2018Article
- N-dodecanoyl-homoserine lactone influences the levels of thiol and proteins related to oxidation-reduction process in Salmonella.PloS one · 2018Article
- Transient Receptor Potential Canonical Channels 4 and 5 MediateOxidative medicine and cellular longevity · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The thiol-disulfide oxidoreductase CXXC catalytic domain of thioredoxin contributes to antioxidant defense in phylogenetically diverse organisms. We find that although the oxidoreductase activity of thioredoxin-1 protects Salmonella enterica serovar Typhimurium from hydrogen peroxide in vitro, it does not appear to contribute to Salmonella's antioxidant defenses in vivo. Nonetheless, thioredoxin-1 defends Salmonella from oxidative stress resulting from NADPH phagocyte oxidase macrophage expression during the innate immune response in mice. Thioredoxin-1 binds to the flexible linker, which connects the receiver and effector domains of SsrB, thereby keeping this response regulator in the soluble fraction. Thioredoxin-1, independently of thiol-disulfide exchange, activates intracellular SPI2 gene transcription required for Salmonella resistance to both reactive species generated by NADPH phagocyte oxidase and oxygen-independent lysosomal host defenses. These findings suggest that the horizontally acquired virulence determinant SsrB is regulated post-translationally by ancestrally present thioredoxin.
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