<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7</volume><submitter>Cheng C</submitter><pubmed_abstract>Microbes employ the thioredoxin system to defend against oxidative stress and ensure correct disulfide bonding to maintain protein function. &lt;i>Listeria monocytogenes&lt;/i> has been shown to encode a putative thioredoxin, TrxA, but its biological roles and underlying mechanisms remain unknown. Here, we showed that expression of &lt;i>L. monocytogenes&lt;/i> TrxA is significantly induced in bacteria treated with the thiol-specific oxidizing agent, diamide. Deletion of &lt;i>trxA&lt;/i> markedly compromised tolerance of the pathogen to diamide, and mainly impaired early stages of infection in human intestinal epithelial Caco-2 cells. In addition, most &lt;i>trxA&lt;/i> mutant bacteria were not associated with polymerized actin, and the rare bacteria that were associated with polymerized actin displayed very sho</pubmed_abstract><journal>Frontiers in cellular and infection microbiology</journal><pagination>287</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5487381</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Thioredoxin A Is Essential for Motility and Contributes to Host Infection of &lt;i>Listeria monocytogenes&lt;/i> via Redox Interactions.</pubmed_title><pmcid>PMC5487381</pmcid><pubmed_authors>Cheng C</pubmed_authors><pubmed_authors>Jiang L</pubmed_authors><pubmed_authors>Freitag NE</pubmed_authors><pubmed_authors>Dong Z</pubmed_authors><pubmed_authors>Huang H</pubmed_authors><pubmed_authors>Han X</pubmed_authors><pubmed_authors>Wang H</pubmed_authors><pubmed_authors>Ma T</pubmed_authors><pubmed_authors>Song H</pubmed_authors><pubmed_authors>Shao C</pubmed_authors><pubmed_authors>Yang Y</pubmed_authors><pubmed_authors>Chen Z</pubmed_authors><pubmed_authors>Fang W</pubmed_authors><pubmed_authors>Wang X</pubmed_authors><pubmed_authors>Sun J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Thioredoxin A Is Essential for Motility and Contributes to Host Infection of &lt;i>Listeria monocytogenes&lt;/i> via Redox Interactions.</name><description>Microbes employ the thioredoxin system to defend against oxidative stress and ensure correct disulfide bonding to maintain protein function. &lt;i>Listeria monocytogenes&lt;/i> has been shown to encode a putative thioredoxin, TrxA, but its biological roles and underlying mechanisms remain unknown. Here, we showed that expression of &lt;i>L. monocytogenes&lt;/i> TrxA is significantly induced in bacteria treated with the thiol-specific oxidizing agent, diamide. Deletion of &lt;i>trxA&lt;/i> markedly compromised tolerance of the pathogen to diamide, and mainly impaired early stages of infection in human intestinal epithelial Caco-2 cells. In addition, most &lt;i>trxA&lt;/i> mutant bacteria were not associated with polymerized actin, and the rare bacteria that were associated with polymerized actin displayed very sho</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017</publication><modification>2025-05-29T19:05:06.274Z</modification><creation>2025-05-29T19:05:06.274Z</creation></dates><accession>S-EPMC5487381</accession><cross_references><pubmed>28702378</pubmed><doi>10.3389/fcimb.2017.00287</doi></cross_references></HashMap>