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Here, we have re-investigated the physiological role of the molybdenum-containing DmsABC dimethyl sulfoxide (DMSO) reductase from\n                      <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                      , which has a proposed role in anaerobic respiration with DMSO. Our investigation into potential physiological substrates revealed that DmsABC efficiently reduces pyrimidine N-oxide, nicotinamide N-oxide, and methionine sulfoxide, and exposure to host cell-produced stressors such as hypochlorite or hydrogen peroxide specifically increased expression of the\n                      <jats:italic toggle=\"yes\">E. coli dmsA<\/jats:italic>\n                      gene.\n                      <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                      strains lacking\n                      <jats:italic toggle=\"yes\">dmsA<\/jats:italic>\n                      showed increased lag times in the presence of hypochlorite, and these strains also showed up to a 90% reduction in adherence to human bladder cells. Interestingly, in the presence of hypochlorite, expression of multiple alternative S-\/N-oxide reductases present in\n                      <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                      was elevated by 2- to 4-fold in a \u2206\n                      <jats:italic toggle=\"yes\">dmsA<\/jats:italic>\n                      strain compared to the wild-type strain, suggesting functional redundancy. The phenotypes of the\n                      <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                      \u2206\n                      <jats:italic toggle=\"yes\">dmsA<\/jats:italic>\n                      strains were strikingly similar to \u2206\n                      <jats:italic toggle=\"yes\">dmsA<\/jats:italic>\n                      strains of the respiratory pathogen\n                      <jats:italic toggle=\"yes\">Haemophilus influenzae<\/jats:italic>\n                      , which confirms the role of both enzymes in supporting host-pathogen interactions. We propose that this function is conserved in enzymes closely related to\n                      <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                      DmsABC. Our study also uncovered that the expression of many\n                      <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                      Mo enzymes was induced by oxidative stressors, including metals such as copper, and further work should be directed at determining the connection of these enzymes to host-pathogen interactions.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        Bacterial urinary tract infections are debilitating and frequently recurring in human populations worldwide, and\n                        <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                        strains are a major cause of these infections. In this study, we have uncovered a new mechanism by which\n                        <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                        can avoid being killed by the human immune system. The bacteria use a set of seven related enzymes that can reverse damage to essential cell components such as amino acids, vitamins, and DNA building blocks. Antibacterial compounds produced by the human immune system specifically induced the production of these enzymes, confirming that they play a role in helping\n                        <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                        survive during infection and making these enzymes potential future drug targets.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/jb.00463-24","type":"journal-article","created":{"date-parts":[[2025,4,14]],"date-time":"2025-04-14T12:14:21Z","timestamp":1744632861000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":8,"title":["Beyond anaerobic respiration\u2014new physiological roles for DmsABC and other S-\/N-oxide reductases in\n                    <i>Escherichia 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