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Characterization of the naturally occurring oxacillinase of Acinetobacter baumannii.


ABSTRACT: A chromosomally encoded oxacillinase, OXA-69, was characterized from Acinetobacter baumannii AYE. beta-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.

SUBMITTER: Heritier C 

PROVIDER: S-EPMC1251506 | biostudies-literature | 2005 Oct

REPOSITORIES: biostudies-literature

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Characterization of the naturally occurring oxacillinase of Acinetobacter baumannii.

Héritier Claire C   Poirel Laurent L   Fournier Pierre-Edouard PE   Claverie Jean-Michel JM   Raoult Didier D   Nordmann Patrice P  

Antimicrobial agents and chemotherapy 20051001 10


A chromosomally encoded oxacillinase, OXA-69, was characterized from Acinetobacter baumannii AYE. beta-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 bl  ...[more]

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