BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa.

@article{Poirel2005BEL1AN,
  title={BEL-1, a novel clavulanic acid-inhibited extended-spectrum beta-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa.},
  author={Laurent Poirel and Laura Bri{\~n}as and Annemie Verlinde and Louis Ide and Patrice L. Nordmann},
  journal={Antimicrobial agents and chemotherapy},
  year={2005},
  volume={49 9},
  pages={3743-8}
}
Screening by a double-disk synergy test identified a Pseudomonas aeruginosa isolate that produced a clavulanic acid-inhibited expanded-spectrum beta-lactamase (ESBL). Cloning and sequencing identified a novel ESBL, BEL-1, weakly related to other Ambler class A ESBLs. beta-Lactamase BEL-1 hydrolyzed significantly most expanded-spectrum cephalosporins and aztreonam, and its activity was inhibited by clavulanic acid, tazobactam, cefoxitin, moxalactam, and imipenem. This chromosome-encoded ESBL… CONTINUE READING
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