{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T16:28:15Z","timestamp":1772209695119,"version":"3.50.1"},"reference-count":102,"publisher":"Public Library of Science (PLoS)","issue":"11","license":[{"start":{"date-parts":[[2020,11,20]],"date-time":"2020-11-20T00:00:00Z","timestamp":1605830400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"abstract":"<jats:p>\n                    Identification of bacterial virulence factors is critical for understanding disease pathogenesis, drug discovery and vaccine development. In this study we used two approaches to predict virulence factors of\n                    <jats:italic>Burkholderia pseudomallei<\/jats:italic>\n                    , the Gram-negative bacterium that causes melioidosis.\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    is naturally antibiotic resistant and there are no clinically available melioidosis vaccines. To identify\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    protein targets for drug discovery and vaccine development, we chose to search for substrates of the\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    periplasmic disulfide bond forming protein A (DsbA). DsbA introduces disulfide bonds into extra-cytoplasmic proteins and is essential for virulence in many Gram-negative organism, including\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    . The first approach to identify\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    DsbA virulence factor substrates was a large-scale genomic analysis of 511 unique\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    disease-associated strains. This yielded 4,496 core gene products, of which we hypothesise 263 are DsbA substrates. Manual curation and database screening of the 263 mature proteins yielded 81 associated with disease pathogenesis or virulence. These were screened for structural homologues to predict potential B-cell epitopes. In the second approach, we searched the\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    genome for homologues of the more than 90 known DsbA substrates in other bacteria. Using this approach, we identified 15 putative\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    DsbA virulence factor substrates, with two of these previously identified in the genomic approach, bringing the total number of putative DsbA virulence factor substrates to 94. The two putative\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    virulence factors identified by both methods are homologues of PenI family \u03b2-lactamase and a molecular chaperone. These two proteins could serve as high priority targets for future\n                    <jats:italic>B<\/jats:italic>\n                    .\n                    <jats:italic>pseudomallei<\/jats:italic>\n                    virulence factor characterization.\n                  <\/jats:p>","DOI":"10.1371\/journal.pone.0241306","type":"journal-article","created":{"date-parts":[[2020,11,20]],"date-time":"2020-11-20T13:38:47Z","timestamp":1605879527000},"page":"e0241306","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":5,"title":["Prediction of Burkholderia pseudomallei DsbA substrates identifies potential virulence factors and vaccine targets"],"prefix":"10.1371","volume":"15","author":[{"given":"Ben","family":"Vezina","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guillaume A.","family":"Petit","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9225-8863","authenticated-orcid":true,"given":"Jennifer L.","family":"Martin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4407-5269","authenticated-orcid":true,"given":"Maria A.","family":"Halili","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2020,11,20]]},"reference":[{"issue":"9370","key":"pone.0241306.ref001","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1016\/S0140-6736(03)13374-0","article-title":"Melioidosis.","volume":"361","author":"NJ White","year":"2003","journal-title":"The Lancet"},{"issue":"5","key":"pone.0241306.ref002","doi-asserted-by":"crossref","first-page":"327","DOI":"10.31128\/AJGP-04-18-4558","article-title":"Melioidosis: An updated review.","volume":"48","author":"A Chakravorty","year":"2019","journal-title":"Aust J Gen Pract"},{"key":"pone.0241306.ref003","doi-asserted-by":"crossref","first-page":"17107","DOI":"10.1038\/nrdp.2017.107","article-title":"Melioidosis.","volume":"4","author":"WJ Wiersinga","year":"2018","journal-title":"Nat Rev Dis Primers"},{"key":"pone.0241306.ref004","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.mib.2015.11.007","article-title":"Intracellular replication of the well-armed pathogen Burkholderia pseudomallei","volume":"29","author":"SJ Willcocks","year":"2016","journal-title":"Curr Opin Microbiol"},{"issue":"4","key":"pone.0241306.ref005","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.00068-18","article-title":"Determinants of extreme \u03b2-Lactam tolerance in the Burkholderia pseudomallei complex","volume":"62","author":"K Held","year":"2018","journal-title":"Antimicrob Agents Chemother"},{"issue":"5","key":"pone.0241306.ref006","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01357-17","article-title":"Mechanisms of resistance to folate pathway inhibitors in Burkholderia pseudomallei: Deviation from the norm.","volume":"8","author":"NL Podnecky","year":"2017","journal-title":"mBio"},{"key":"pone.0241306.ref007","doi-asserted-by":"crossref","first-page":"305","DOI":"10.3389\/fmicb.2015.00305","article-title":"Efflux pump-mediated drug resistance in Burkholderia.","volume":"6","author":"NL Podnecky","year":"2015","journal-title":"Front Microbiol"},{"key":"pone.0241306.ref008","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.drup.2016.07.003","article-title":"Antibiotic resistance in Burkholderia species","volume":"28","author":"KA Rhodes","year":"2016","journal-title":"Drug Resist Updat"},{"issue":"12","key":"pone.0241306.ref009","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.2217\/fmb.12.116","article-title":"Mechanisms of antibiotic resistance in Burkholderia pseudomallei: implications for treatment of melioidosis.","volume":"7","author":"HP Schweizer","year":"2012","journal-title":"Future Microbiol"},{"issue":"4","key":"pone.0241306.ref010","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/j.ijantimicag.2014.01.005","article-title":"prophylaxis of melioidosis","volume":"43","author":"Dance D. 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