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

  1. Poirel, L. 1
  2. Brinas, L. 1
  3. Verlinde, A. 3
  4. Ide, Louis. 3
  5. Nordmann, P. 1
  1. 1 Hôpital de Bicêtre, Faculté de Médecine Paris-Sud, Université Paris XI, Le Kremlin-Bicêtre, France
  2. 2 Area de Bioquimica y Biologia Molecular, Universidad de la Rioja, 26006 Logrono, Spain
  3. 3 Department of Microbiology, Heilig Hartziekenhuis Roeselare, Wilgenstraat 2, 8800 Roeselare, Belgium
  4. 4 Service de Bactériologie-Virologie, Hôpital de Bicêtre, 78 rue du Genéral Leclerc, 94275 Le Kremlin-Bicêtre Cedex, France
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Revista:
Antimicrobial Agents and Chemotherapy

ISSN: 0066-4804

Año de publicación: 2005

Volumen: 49

Número: 9

Páginas: 3743-3748

Tipo: Artículo

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DOI: 10.1128/AAC.49.9.3743-3748.2005 PMID: 16127048 SCOPUS: 2-s2.0-24144502900 WoS: WOS:000231542900021 DIALNET GOOGLE SCHOLAR lock_openAcceso abierto editor

Otras publicaciones en: Antimicrobial Agents and Chemotherapy

Repositorio institucional: lock_openAcceso abierto Editor

Resumen

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.