4.7 Article

Characterization of the naturally occurring oxacillinase of Acinetobacter baumannii

Journal

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 49, Issue 10, Pages 4174-4179

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.49.10.4174-4179.2005

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A chromosomally encoded oxacillinase, OXA-69, was characterized from Acinetobacter baumannii AYE. P-Lactamase OXA-69 shared 97% amino acid identity with the recently described OXA-51 enzyme of A. baumannii and 62 and 56% amino acid identity with the carbapenem-hydrolyzing oxacillinases OXA-24 and OXA-23, respectively. Biochemical characterization of the purified OXA-69 revealed a narrow-spectrum hydrolysis profile but including, at a low level, imipenem and meropenem. By PCR and sequencing bla(OXA-69)-like genes were identified in all A. baumannii strains tested (n = 12), suggesting that this oxacillinase is naturally occurring in that species.

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