{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T00:41:01Z","timestamp":1790988061549,"version":"4.1.0"},"reference-count":24,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2009,7,1]],"date-time":"2009-07-01T00:00:00Z","timestamp":1246406400000},"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":[[2009,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The glycopeptide vancomycin is a drug of last resort for infection with gram-positive organisms, and three genes are vital to resistance:\n            <jats:italic>vanH<\/jats:italic>\n            ,\n            <jats:italic>vanA<\/jats:italic>\n            , and\n            <jats:italic>vanX<\/jats:italic>\n            . These genes are found in a\n            <jats:italic>vanHAX<\/jats:italic>\n            cluster, which is conserved across pathogenic bacteria, glycopeptide antibiotic producers, and other environmental bacteria. The genome sequence of the anaerobic, gram-positive, dehalogenating bacterium\n            <jats:italic>Desulfitobacterium hafniense<\/jats:italic>\n            Y51 revealed a predicted\n            <jats:italic>vanA<\/jats:italic>\n            homolog; however, it exists in a\n            <jats:italic>vanAWK-murFX<\/jats:italic>\n            cluster, unlike those of other vancomycin-resistant organisms. Using purified recombinant VanA from\n            <jats:italic>D. hafniense<\/jats:italic>\n            Y51, we determined its substrate specificity and found it to have a 42-fold preference for\n            <jats:sc>d<\/jats:sc>\n            -lactate over\n            <jats:sc>d<\/jats:sc>\n            -alanine, confirming its activity as a\n            <jats:sc>d<\/jats:sc>\n            -Ala-\n            <jats:sc>d<\/jats:sc>\n            -Lac ligase and its annotation as VanA. Furthermore, we showed that\n            <jats:italic>D. hafniense<\/jats:italic>\n            Y51 is highly resistant to vancomycin, with a MIC for growth of 64 \u03bcg\/ml. Finally,\n            <jats:italic>\n              vanA\n              <jats:sub>Dh<\/jats:sub>\n            <\/jats:italic>\n            is expressed during growth in vancomycin, as demonstrated by reverse transcription-PCR. This finding represents a new glycopeptide antibiotic resistance gene cluster and expands the genetic diversity of resistance to this important class of antibiotic.\n          <\/jats:p>","DOI":"10.1128\/aac.01408-08","type":"journal-article","created":{"date-parts":[[2009,5,5]],"date-time":"2009-05-05T01:29:27Z","timestamp":1241486967000},"page":"2841-2845","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":10,"title":["Noncanonical Vancomycin Resistance Cluster from\n            <i>Desulfitobacterium hafniense<\/i>\n            Y51"],"prefix":"10.1128","volume":"53","author":[{"given":"Lindsay","family":"Kalan","sequence":"first","affiliation":[{"name":"Michael G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara","family":"Ebert","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tom","family":"Kelly","sequence":"additional","affiliation":[{"name":"Department of Microbiology, St. Josephs' Health Care, Hamilton, Ontario, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerard D.","family":"Wright","sequence":"additional","affiliation":[{"name":"Michael G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.37.8.1563"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.174.8.2582-2591.1992"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/bti206"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00107a007"},{"key":"e_1_3_2_6_2","unstructured":"Methods for antimicrobial susceptibility testing of anaerobic bacteria 7th ed. 2007 27"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1120800"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2003.03289.x"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.2006.00270.x"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.48.12.4915-4918.2004"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.49.10.4227-4233.2005"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M413801200"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2004.04032.x"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1021\/cr030103a"},{"key":"e_1_3_2_15_2","unstructured":"GraFit 4.0.21. 1992"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1086\/491709"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1006\/meth.2001.1262"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.42.9.2215"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.188.6.2262-2274.2006"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.102285099"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3010005"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2006.00029.x"},{"key":"e_1_3_2_23_2","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1021\/bi00845a007","volume":"7","year":"1968","unstructured":"Wampler, D. E., and E. W. Westhead. 1968. Two aspartokinases from Escherichia coli. Nature of the inhibition and molecular changes accompanying reversible inactivation. 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