Biochemical and genetic characterization of carbapenem-hydrolyzing β-lactamase OXA-229 from Acinetobacter bereziniae

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Abstract

Acinetobacter bereziniae (formerly Acinetobacter genomospecies 10) isolate Nec was recovered from a skin sample of a patient hospitalized in Paris, France. It was resistant to penicillins, penicillin-inhibitor combinations, and carbapenems. Cloning and expression in Escherichia coli identified the carbapenem-hydrolyzing class D β-lactamase OXA-229, which is weakly related to other oxacillinases (66% amino acid identity with the closest oxacillinase, OXA-58). It hydrolyzed penicillins, oxacillin, and imipenem but not expanded-spectrum cephalosporins. Sequencing of the genetic context of the blaOXA-229 gene did not identify an insertion sequence but did identify mutations in the promoter sequences in comparison to the fully susceptible A. bereziniae reference strain. The overexpression of blaOXA-229 in A. bereziniae Nec as a source of carbapenem resistance was identified by quantitative real-time PCR. Copyright © 2012, American Society for Microbiology. All Rights Reserved.

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Bonnin, R. A., Ocampo-Sosa, A. A., Poirel, L., Guet-Revillet, H., & Nordmann, P. (2012). Biochemical and genetic characterization of carbapenem-hydrolyzing β-lactamase OXA-229 from Acinetobacter bereziniae. Antimicrobial Agents and Chemotherapy, 56(7), 3923–3927. https://doi.org/10.1128/AAC.00257-12

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