{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T06:43:47Z","timestamp":1789195427923,"version":"build-2803163510"},"reference-count":35,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2006,11,1]],"date-time":"2006-11-01T00:00:00Z","timestamp":1162339200000},"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":[[2006,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Vancomycin resistance of\n            <jats:italic>Staphylococcus aureus<\/jats:italic>\n            NY-VRSA and VRSA-5 is due to acquisition of a\n            <jats:italic>vanA<\/jats:italic>\n            operon located in a Tn\n            <jats:italic>1546<\/jats:italic>\n            -like element. The\n            <jats:italic>vanA<\/jats:italic>\n            gene cluster of NY-VRSA contained one copy of insertion sequences IS\n            <jats:italic>1251<\/jats:italic>\n            and IS\n            <jats:italic>1216V<\/jats:italic>\n            relative to that of VRSA-5. As evidenced by the nature of the late peptidoglycan precursors and by quantification of\n            <jats:sc>d<\/jats:sc>\n            ,\n            <jats:sc>d<\/jats:sc>\n            -peptidase activities, the vancomycin resistance genes were efficiently expressed in both strains. Study of the stability and inducibility of glycopeptide resistance suggested that low-level glycopeptide resistance of NY-VRSA was most probably due to plasmid instability combined with a long delay for resistance induction. The activity of combinations of vancomycin or teicoplanin with oxacillin against the four VanA-type\n            <jats:italic>S. aureus<\/jats:italic>\n            strains already reported was tested by single and double disk diffusion, E-test on agar alone or supplemented with antibiotics, the checkerboard technique, and by determining time-kill curves. A strong synergism against the four clinical isolates, with fractional inhibitory concentration indexes from 0.008 to 0.024, was reproducibly observed between the two antibiotics by all methods. These observations indicate that cell wall inhibitors of the \u03b2-lactam and glycopeptide classes exert strong and mutual antagonistic effects on resistance to each other against VanA-type methicillin-resistant\n            <jats:italic>S. aureus<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/aac.00410-06","type":"journal-article","created":{"date-parts":[[2006,10,25]],"date-time":"2006-10-25T20:58:50Z","timestamp":1161809930000},"page":"3622-3630","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":58,"title":["Synergism between \u03b2-Lactams and Glycopeptides against VanA-Type Methicillin-Resistant\n            <i>Staphylococcus aureus<\/i>\n            and Heterologous Expression of the\n            <i>vanA<\/i>\n            Operon"],"prefix":"10.1128","volume":"50","author":[{"given":"Bruno","family":"Pe\u0301richon","sequence":"first","affiliation":[{"name":"Unite\u0301 des Agents Antibacte\u0301riens, Institut Pasteur, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrice","family":"Courvalin","sequence":"additional","affiliation":[{"name":"Unite\u0301 des Agents Antibacte\u0301riens, Institut Pasteur, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1093\/jac\/dkh350","volume":"54","year":"2004","unstructured":"Adhikari, R. 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