{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T03:42:37Z","timestamp":1777434157046,"version":"3.51.4"},"reference-count":73,"publisher":"SAGE Publications","issue":"4","license":[{"start":{"date-parts":[[2014,2,1]],"date-time":"2014-02-01T00:00:00Z","timestamp":1391212800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Antioxidants &amp; Redox Signaling"],"published-print":{"date-parts":[[2014,2]]},"abstract":"<jats:p>\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Aims:<\/jats:italic>\n                    <\/jats:bold>\n                    The intracellular pathogen\n                    <jats:italic toggle=\"yes\">Burkholderia pseudomallei<\/jats:italic>\n                    causes the disease melioidosis, a major source of morbidity and mortality in southeast Asia and northern Australia. The need to develop novel antimicrobials is compounded by the absence of a licensed vaccine and the bacterium's resistance to multiple antibiotics. In a number of clinically relevant Gram-negative pathogens, DsbA is the primary disulfide oxidoreductase responsible for catalyzing the formation of disulfide bonds in secreted and membrane-associated proteins. In this study, a putative\n                    <jats:italic toggle=\"yes\">B. pseudomallei dsbA<\/jats:italic>\n                    gene was evaluated functionally and structurally and its contribution to infection assessed.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Results:<\/jats:italic>\n                    <\/jats:bold>\n                    Biochemical studies confirmed the\n                    <jats:italic toggle=\"yes\">dsbA<\/jats:italic>\n                    gene encodes a protein disulfide oxidoreductase. A\n                    <jats:italic toggle=\"yes\">dsbA<\/jats:italic>\n                    deletion strain of\n                    <jats:italic toggle=\"yes\">B. pseudomallei<\/jats:italic>\n                    was attenuated in both macrophages and a BALB\/c mouse model of infection and displayed pleiotropic phenotypes that included defects in both secretion and motility. The 1.9 \u00c5 resolution crystal structure of BpsDsbA revealed differences from the classic member of this family\n                    <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                    DsbA, in particular within the region surrounding the active site disulfide where EcDsbA engages with its partner protein\n                    <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                    DsbB, indicating that the interaction of BpsDsbA with its proposed partner BpsDsbB may be distinct from that of EcDsbA-EcDsbB.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Innovation:<\/jats:italic>\n                    <\/jats:bold>\n                    This study has characterized BpsDsbA biochemically and structurally and determined that it is required for virulence of\n                    <jats:italic toggle=\"yes\">B. pseudomallei.<\/jats:italic>\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Conclusion:<\/jats:italic>\n                    <\/jats:bold>\n                    These data establish a critical role for BpsDsbA in\n                    <jats:italic toggle=\"yes\">B. pseudomallei<\/jats:italic>\n                    infection, which in combination with our structural characterization of BpsDsbA will facilitate the future development of rationally designed inhibitors against this drug-resistant organism.\n                    <jats:italic toggle=\"yes\">Antioxid. Redox Signal.<\/jats:italic>\n                    20, 606\u2013617.\n                  <\/jats:p>","DOI":"10.1089\/ars.2013.5375","type":"journal-article","created":{"date-parts":[[2013,7,31]],"date-time":"2013-07-31T14:18:04Z","timestamp":1375280284000},"page":"606-617","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":55,"title":["Disarming\n                    <i>Burkholderia pseudomallei<\/i>\n                    : Structural and Functional Characterization of a Disulfide Oxidoreductase (DsbA) Required for Virulence\n                    <i>In Vivo<\/i>"],"prefix":"10.1177","volume":"20","author":[{"given":"Philip M.","family":"Ireland","sequence":"first","affiliation":[{"name":"Defence Science and Technology Laboratory","place":["United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R\u00f3is\u00edn M.","family":"McMahon","sequence":"additional","affiliation":[{"name":"The University of Queensland","place":["Australia"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laura E.","family":"Marshall","sequence":"additional","affiliation":[{"name":"Defence Science and Technology Laboratory","place":["United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria","family":"Halili","sequence":"additional","affiliation":[{"name":"The University of Queensland","place":["Australia"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emily","family":"Furlong","sequence":"additional","affiliation":[{"name":"The University of Queensland","place":["Australia"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephanie","family":"Tay","sequence":"additional","affiliation":[{"name":"The University of Queensland","place":["Australia"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jennifer L.","family":"Martin","sequence":"additional","affiliation":[{"name":"The University of Queensland","place":["Australia"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mitali","family":"Sarkar-Tyson","sequence":"additional","affiliation":[{"name":"Defence Science and Technology Laboratory","place":["United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[2014,2,1]]},"reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1042\/BST0391327"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444909052925"},{"issue":"8","key":"e_1_3_3_4_2","article-title":"The Phenix refinement framework","volume":"42","author":"Afonine PVG-KRWAPD","year":"2005","unstructured":"Afonine PVG-KRWAPD. 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