{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T12:46:17Z","timestamp":1760013977794},"reference-count":43,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2011,2,1]],"date-time":"2011-02-01T00:00:00Z","timestamp":1296518400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2011,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Previous studies have shown that the O polysaccharides (OPS) expressed by\n            <jats:italic>Burkholderia mallei<\/jats:italic>\n            are similar to those produced by\n            <jats:italic>Burkholderia thailandensis<\/jats:italic>\n            except that they lack the 4-\n            <jats:italic>O<\/jats:italic>\n            -acetyl modifications on their 6-deoxy-\u03b1-\n            <jats:sc>l<\/jats:sc>\n            -talopyranosyl residues. In the present study, we describe the identification and characterization of an open reading frame, designated\n            <jats:italic>oacA<\/jats:italic>\n            , expressed by\n            <jats:italic>B. thailandensis<\/jats:italic>\n            that accounts for this phenomenon. Utilizing the\n            <jats:italic>B. thailandensis<\/jats:italic>\n            and\n            <jats:italic>B. mallei<\/jats:italic>\n            lipopolysaccharide (LPS)-specific monoclonal antibodies Pp-PS-W and 3D11, Western immunoblot analyses demonstrated that the LPS antigens expressed by the\n            <jats:italic>oacA<\/jats:italic>\n            mutant,\n            <jats:italic>B. thailandensis<\/jats:italic>\n            ZT0715, were antigenically similar to those produced by\n            <jats:italic>B. mallei<\/jats:italic>\n            ATCC 23344. In addition, immunoblot analyses demonstrated that when\n            <jats:italic>B. mallei<\/jats:italic>\n            ATCC 23344 was complemented in\n            <jats:italic>trans<\/jats:italic>\n            with\n            <jats:italic>oacA<\/jats:italic>\n            , it synthesized\n            <jats:italic>B. thailandensis<\/jats:italic>\n            -like LPS antigens. To elucidate the structure of the OPS moieties expressed by ZT0715, purified samples were analyzed via nuclear magnetic resonance spectroscopy. As predicted, these studies demonstrated that the loss of OacA activity influenced the O acetylation phenotype of the OPS moieties. Unexpectedly, however, the results indicated that the O methylation status of the OPS antigens was also affected by the loss of OacA activity. Nonetheless, it was revealed that the LPS moieties expressed by the\n            <jats:italic>oacA<\/jats:italic>\n            mutant reacted strongly with the\n            <jats:italic>B. mallei<\/jats:italic>\n            LPS-specific protective monoclonal antibody 9C1-2. Based on these findings, it appears that OacA is required for the 4-\n            <jats:italic>O<\/jats:italic>\n            acetylation and 2-\n            <jats:italic>O<\/jats:italic>\n            methylation of\n            <jats:italic>B. thailandensis<\/jats:italic>\n            OPS antigens and that ZT0715 may provide a safe and cost-effective source of\n            <jats:italic>B. mallei<\/jats:italic>\n            -like OPS to facilitate the synthesis of glanders subunit vaccine candidates.\n          <\/jats:p>","DOI":"10.1128\/iai.01023-10","type":"journal-article","created":{"date-parts":[[2010,11,30]],"date-time":"2010-11-30T05:12:27Z","timestamp":1291093947000},"page":"961-969","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":24,"title":["<i>Burkholderia thailandensis oacA<\/i>\n            Mutants Facilitate the Expression of\n            <i>Burkholderia mallei<\/i>\n            -Like O Polysaccharides"],"prefix":"10.1128","volume":"79","author":[{"given":"Paul J.","family":"Brett","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, University of South Alabama, Mobile, Alabama 36688"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mary N.","family":"Burtnick","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of South Alabama, Mobile, Alabama 36688"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christian","family":"Heiss","sequence":"additional","affiliation":[{"name":"Complex Carbohydrate Research Center, The University of Georgia, Athens, Georgia 30602"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Parastoo","family":"Azadi","sequence":"additional","affiliation":[{"name":"Complex Carbohydrate Research Center, The University of Georgia, Athens, Georgia 30602"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David","family":"DeShazer","sequence":"additional","affiliation":[{"name":"Bacteriology Division, United States Army Medical Research Institute of Infectious Diseases, Fort Detrick, Maryland 21702"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Donald E.","family":"Woods","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Infectious Diseases, University of Calgary Health Sciences Centre, Calgary, Alberta, T2N 4N1, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Frank C.","family":"Gherardini","sequence":"additional","affiliation":[{"name":"Laboratory of Zoonotic Pathogens, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, Montana 59840"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1348-0421.2002.tb02679.x"},{"key":"e_1_3_2_3_2","first-page":"1578","year":"1998","unstructured":"Bartlett, J. 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