BEL-1, a novel clavulanic acid-inhibited extended-spectrum ß-lactamase, and the class 1 integron In120 in Pseudomonas aeruginosa
- Poirel, L. 1
- Brinas, L. 1
- Verlinde, A. 3
- Ide, Louis. 3
- Nordmann, P. 1
- 1 Hôpital de Bicêtre, Faculté de Médecine Paris-Sud, Université Paris XI, Le Kremlin-Bicêtre, France
- 2 Area de Bioquimica y Biologia Molecular, Universidad de la Rioja, 26006 Logrono, Spain
- 3 Department of Microbiology, Heilig Hartziekenhuis Roeselare, Wilgenstraat 2, 8800 Roeselare, Belgium
- 4 Service de Bactériologie-Virologie, Hôpital de Bicêtre, 78 rue du Genéral Leclerc, 94275 Le Kremlin-Bicêtre Cedex, France
ISSN: 0066-4804
Argitalpen urtea: 2005
Alea: 49
Zenbakia: 9
Orrialdeak: 3743-3748
Mota: Artikulua
Beste argitalpen batzuk: Antimicrobial Agents and Chemotherapy
Laburpena
Screening by a double-disk synergy test identified a Pseudomonas aeruginosa isolate that produced a clavulanic acid-inhibited expanded-spectrum β-lactamase (ESBL). Cloning and sequencing identified a novel ESBL, BEL-1, weakly related to other Ambler class A ESBLs. β-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 gene was embedded in a class 1 integron containing three other gene cassettes. In addition, this integron was bracketed by Tn1404 transposon sequences at its right end and by P. aeruginosa-specific sequences at its left end. Copyright © 2005, American Society for Microbiology. All Rights Reserved.