{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7"],"submitter":["Cheng C"],"pubmed_abstract":["Microbes employ the thioredoxin system to defend against oxidative stress and ensure correct disulfide bonding to maintain protein function. <i>Listeria monocytogenes</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 <i>L. monocytogenes</i> TrxA is significantly induced in bacteria treated with the thiol-specific oxidizing agent, diamide. Deletion of <i>trxA</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 <i>trxA</i> mutant bacteria were not associated with polymerized actin, and the rare bacteria that were associated with polymerized actin displayed very sho"],"journal":["Frontiers in cellular and infection microbiology"],"pagination":["287"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5487381"],"repository":["biostudies-literature"],"pubmed_title":["Thioredoxin A Is Essential for Motility and Contributes to Host Infection of <i>Listeria monocytogenes</i> via Redox Interactions."],"pmcid":["PMC5487381"],"pubmed_authors":["Cheng C","Jiang L","Freitag NE","Dong Z","Huang H","Han X","Wang H","Ma T","Song H","Shao C","Yang Y","Chen Z","Fang W","Wang X","Sun J"],"additional_accession":[]},"is_claimable":false,"name":"Thioredoxin A Is Essential for Motility and Contributes to Host Infection of <i>Listeria monocytogenes</i> via Redox Interactions.","description":"Microbes employ the thioredoxin system to defend against oxidative stress and ensure correct disulfide bonding to maintain protein function. <i>Listeria monocytogenes</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 <i>L. monocytogenes</i> TrxA is significantly induced in bacteria treated with the thiol-specific oxidizing agent, diamide. Deletion of <i>trxA</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 <i>trxA</i> mutant bacteria were not associated with polymerized actin, and the rare bacteria that were associated with polymerized actin displayed very sho","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017","modification":"2025-05-29T19:05:06.274Z","creation":"2025-05-29T19:05:06.274Z"},"accession":"S-EPMC5487381","cross_references":{"pubmed":["28702378"],"doi":["10.3389/fcimb.2017.00287"]}}