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Characterization of the Naturally Occurring Oxacillinase ofAcinetobacter baumannii
Author(s) -
Claire Héritier,
Laurent Poirel,
PierreEdouard Fournier,
JeanMichel Claverie,
Didier Raoult,
Patrice Nordmann
Publication year - 2005
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.49.10.4174-4179.2005
Subject(s) - acinetobacter baumannii , imipenem , meropenem , microbiology and biotechnology , carbapenem , gene , biology , amino acid , antibiotics , genetics , bacteria , antibiotic resistance , pseudomonas aeruginosa
A chromosomally encoded oxacillinase, OXA-69, was characterized fromAcinetobacter baumannii AYE. β-Lactamase OXA-69 shared 97% amino acid identity with the recently described OXA-51 enzyme ofA. 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 sequencingbla OXA-69 -like genes were identified in allA. baumannii strains tested (n = 12), suggesting that this oxacillinase is naturally occurring in that species.

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