Heterogeneous hydrolytic features for OXA-48-like β-lactamases
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- Oueslati, Saoussen INSERM U914 ‘Emerging Resistance to Antibiotics', K.-Bicêtre, France
- Nordmann, Patrice INSERM U914 ‘Emerging Resistance to Antibiotics', K.-Bicêtre, France
- Poirel, Laurent INSERM U914 ‘Emerging Resistance to Antibiotics', K.-Bicêtre, France
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2015
Published in:
- Journal of Antimicrobial Chemotherapy. - Oxford University Press. - 2015, vol. 70, no. 4, p. 1059-1063
English
Objectives Carbapenem-hydrolysing class D β-lactamases of the OXA-48 type are increasingly reported from Enterobacteriaceae. β-Lactamase OXA-48 hydrolyses penicillins very efficiently, but carbapenems only weakly and spares broad-spectrum cephalosporins. Recently, diverse OXA-48-like β-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. Methods blaOXA-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. Results 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 β-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. Conclusions A detailed comparative analysis of the kinetic properties of the OXA-48-like β-lactamases is provided here. It clarifies the respective features of each OXA-48-like variant and their respective impacts in terms of carbapenem resistance
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License undefined© The Author 2015. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com
- Identifiers
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- RERO DOC 297236
- SWISSBIB (NATIONALLICENCE)oxford-10.1093/jac/dku524
- DOI 10.1093/jac/dku524
- Persistent URL
- https://sonar.ch/global/documents/305737
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