{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T19:11:46Z","timestamp":1791141106602,"version":"4.1.0"},"reference-count":27,"publisher":"American Society for Microbiology","issue":"9","license":[{"start":{"date-parts":[[2003,9,1]],"date-time":"2003-09-01T00:00:00Z","timestamp":1062374400000},"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":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2003,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>As part of the CANCER Antimicrobial Surveillance Program in North America, a clinical strain of<jats:italic>Pseudomonas aeruginosa<\/jats:italic>, strain 07-406, isolated in Texas was found to be resistant to all antimicrobials except polymyxin B. Genetic analysis of this isolate identified two unique extended-spectrum \u03b2-lactamase genes. One,<jats:italic>bla<\/jats:italic><jats:sub>VIM-7<\/jats:sub>, encoded a metallo-\u03b2-lactamase (unpublished data), and the other,<jats:italic>bla<\/jats:italic><jats:sub>OXA-45<\/jats:sub>, described here, encoded a class D extended-spectrum \u03b2-lactamase.<jats:italic>bla<\/jats:italic><jats:sub>OXA-45<\/jats:sub>was isolated on a<jats:italic>Sau<\/jats:italic>3A1 genomic fragment of 1.8 kb and encodes a protein of 264 amino acids with the highest identities to OXA-18 (65.9%), OXA-9 (42.8%), OXA-22 (40.2%), OXA-12 (38.6%), and OXA-29 (35.2%) but weak identities with other class D \u03b2-lactamases.<jats:italic>bla<\/jats:italic><jats:sub>OXA-45<\/jats:sub>was found to be harbored on a 24-kb plasmid in a region that displays high identities with a section of the 43-kb genomic island of<jats:italic>Salmonella enterica<\/jats:italic>serovar Typhimurium DT104. Biochemically OXA-45 is most similar to OXA-18 in its substrate profile and inhibition by clavulanic acid and is a member of the 2d\u2032 class of \u03b2-lactamases.<\/jats:p>","DOI":"10.1128\/aac.47.9.2859-2863.2003","type":"journal-article","created":{"date-parts":[[2003,8,22]],"date-time":"2003-08-22T21:07:12Z","timestamp":1061586432000},"page":"2859-2863","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":48,"title":["Molecular and Biochemical Characterization of OXA-45, an Extended-Spectrum Class 2d\u2032 \u03b2-Lactamase in<i>Pseudomonas aeruginosa<\/i>"],"prefix":"10.1128","volume":"47","author":[{"given":"Mark A.","family":"Toleman","sequence":"first","affiliation":[{"name":"Department of Pathology and Microbiology, University of Bristol, Bristol BS8 1TD, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kenneth","family":"Rolston","sequence":"additional","affiliation":[{"name":"Anderson Medical Center, Houston, Texas"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald N.","family":"Jones","sequence":"additional","affiliation":[{"name":"The JONES Group\/JMI Laboratories, North Liberty, Iowa"},{"name":"the Tufts University School of Medicine, Boston, Massachusetts"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Timothy R.","family":"Walsh","sequence":"additional","affiliation":[{"name":"Department of Pathology and Microbiology, University of Bristol, Bristol BS8 1TD, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_1_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.45.2.583-588.2001"},{"key":"e_1_3_1_3_2","doi-asserted-by":"publisher","DOI":"10.1098\/rstb.1980.0049"},{"key":"e_1_3_1_4_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00239-002-2328-y"},{"key":"e_1_3_1_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.183.19.5725-5732.2001"},{"key":"e_1_3_1_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.14.4.933-951.2001"},{"key":"e_1_3_1_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.6.1211"},{"key":"e_1_3_1_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.8.1881"},{"key":"e_1_3_1_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.41.4.785"},{"key":"e_1_3_1_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.42.12.3117"},{"key":"e_1_3_1_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.45.12.3509-3516.2001"},{"key":"e_1_3_1_12_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.241442898"},{"key":"e_1_3_1_13_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.37.8.1637"},{"key":"e_1_3_1_14_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2920555"},{"key":"e_1_3_1_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1369-5274(00)00128-4"},{"key":"e_1_3_1_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(00)00534-7"},{"key":"e_1_3_1_17_2","doi-asserted-by":"crossref","first-page":"865","DOI":"10.2174\/1381612805666230112185101","volume":"5","year":"1999","unstructured":"Naas, T., and P. 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