ArticleJournal of bacteriology2009
Thioredoxin 1 participates in the activity of the Salmonella enterica serovar Typhimurium pathogenicity island 2 type III secretion system.
Article in Journal of bacteriology, 2009. 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.
- Promiscuity of response regulators for thioredoxin steers bacterial virulence.Nature communications · 2022Article
- Evolution of Copper Homeostasis and Virulence inFrontiers in microbiology · 2022Article
- The extracellular thioredoxin Etrx3 is required for macrophage infection in Rhodococcus equi.Veterinary research · 2020Article
- Responses ofMicroorganisms · 2020Article
- Thioredoxin H (TrxH) contributes to adversity adaptation and pathogenicity of Edwardsiella piscicida.Veterinary research · 2019Article
- Transient Receptor Potential Canonical Channels 4 and 5 MediateOxidative medicine and cellular longevity · 2018Article
- Antioxidant Defense by Thioredoxin Can Occur Independently of Canonical Thiol-Disulfide Oxidoreductase Enzymatic Activity.Cell reports · 2016Article
- Salmonella-how a metabolic generalist adopts an intracellular lifestyle during infection.Frontiers in cellular and infection microbiology · 2014Review
- Article
- Oxidoreductases that act as conditional virulence suppressors in Salmonella enterica serovar Typhimurium.PloS one · 2013Article
- Pathogenicity of Salmonella enterica in Caenorhabditis elegans relies on disseminated oxidative stress in the infected host.PloS one · 2012Article
- Salmonella enterica serovar typhimurium trxA mutants are protective against virulent challenge and induce less inflammation than the live-attenuated vaccine strain SL3261.Infection and immunity · 2010Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The facultative intracellular pathogen Salmonella enterica serovar Typhimurium relies on its Salmonella pathogenicity island 2 (SPI2) type III secretion system (T3SS) for intracellular replication and virulence. We report that the oxidoreductase thioredoxin 1 (TrxA) and SPI2 are coinduced for expression under in vitro conditions that mimic an intravacuolar environment, that TrxA is needed for proper SPI2 activity under these conditions, and that TrxA is indispensable for SPI2 activity in both phagocytic and epithelial cells. Infection experiments in mice demonstrated that SPI2 strongly contributed to virulence in a TrxA-proficient background whereas SPI2 did not affect virulence in a trxA mutant. Complementation analyses using wild-type trxA or a genetically engineered trxA coding for noncatalytic TrxA showed that the catalytic activity of TrxA is essential for SPI2 activity in phagocytic cells whereas a noncatalytic variant of TrxA partially sustained SPI2 activity in epithelial cells and virulence in mice. These results show that TrxA is needed for the intracellular induction of SPI2 and provide new insights into the functional integration between catalytic and noncatalytic activities of TrxA and a bacterial T3SS in different settings of intracellular infections.
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