{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T06:30:37Z","timestamp":1791354637251,"version":"4.3.1"},"reference-count":18,"publisher":"Oxford University Press (OUP)","issue":"4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,4,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Objectives<\/jats:title>\n                    <jats:p>Carbapenem-hydrolysing class D \u03b2-lactamases of the OXA-48 type are increasingly reported from Enterobacteriaceae. \u03b2-Lactamase OXA-48 hydrolyses penicillins very efficiently, but carbapenems only weakly and spares broad-spectrum cephalosporins. Recently, diverse OXA-48-like \u03b2-lactamases have been identified worldwide (OXA-162, OXA-181, OXA-163, OXA-204 and OXA-232). They differ by few amino acid substitutions or by amino acid deletions.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>bla \u00a0OXA-48, blaOXA-162, blaOXA-163, blaOXA-181, blaOXA-204 and blaOXA-232 were cloned into the same expression vector and expressed in the same Escherichia coli background. Kinetic studies were performed with enzymes purified by ion-exchange chromatography. Determination of hydrolytic activities was performed by UV spectrophotometry. MICs were determined for all recombinant strains, using as background either the WT E. coli TOP10 strain or a porin-deficient E. coli strain.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>Kinetic studies showed that OXA-162 and OXA-204 shared the same hydrolytic properties as OXA-48. On the other hand, OXA-181 possessed a higher ability to hydrolyse carbapenems, while OXA-232 hydrolysed those substrates less efficiently. In contrast to the other OXA-48-like \u03b2-lactamases, OXA-163 hydrolysed broad-spectrum cephalosporins very efficiently, but did not possess significant carbapenemase activity. Although several of these OXA-48-like enzymes possess low activity against carbapenems, MICs of carbapenems were significantly elevated when determined for strains possessing permeability defects.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>A detailed comparative analysis of the kinetic properties of the OXA-48-like \u03b2-lactamases is provided here. It clarifies the respective features of each OXA-48-like variant and their respective impacts in terms of carbapenem resistance.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1093\/jac\/dku524","type":"journal-article","created":{"date-parts":[[2015,1,12]],"date-time":"2015-01-12T21:23:25Z","timestamp":1421097805000},"page":"1059-1063","source":"Crossref","is-referenced-by-count":136,"title":["Heterogeneous hydrolytic features for OXA-48-like \u03b2-lactamases"],"prefix":"10.1093","volume":"70","author":[{"given":"Saoussen","family":"Oueslati","sequence":"first","affiliation":[{"name":"1 \u00a0INSERM U914 \u2018Emerging Resistance to Antibiotics\u2019, K.-Bic\u00eatre, France"},{"name":"2 \u00a0LabEx LERMIT, Facult\u00e9 de M\u00e9decine Paris Sud, K.-Bic\u00eatre, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrice","family":"Nordmann","sequence":"additional","affiliation":[{"name":"1 \u00a0INSERM U914 \u2018Emerging Resistance to Antibiotics\u2019, 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