4.7 Article

Molecular and biochemical characterization of ambler class A extended-spectrum β-lactamase CGA-1 from Chryseobacterium gleum

Journal

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 46, Issue 4, Pages 966-970

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.46.4.966-970.2002

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Antibiotic susceptibility testing by disk diffusion of a Chryseobacterium gleum isolate, strain CIP 103039, showed a typical synergy image between clavulanic acid and expanded-spectrum cephalosporins. Shotgun cloning gave a recombinant plasmid in Escherichia coli that produced a beta-lactamase, CGA-1, with a pI value of 8.9 that conferred resistance to most penicillins (except ureidopenicillins) and narrow-spectrum cephalosporins and an intermediate susceptibility to expanded-spectrum cephalosporins and aztreonam. The CGA-1 amino acid sequence shared only 60% amino acid identity with CME-1 and CME-2 from Chryseobacterium meningosepticum, the most closely related beta-lactamases. CGA-1 was very likely chromosome encoded. It is a novel member of the PER subgroup of Ambler class A beta-lactamases (Bush functional group 2be).

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