Characterization of DIM-1, an Integron-Encoded Metallo-β-Lactamase from a Pseudomonas stutzeri Clinical Isolate in the Netherlands

Author:

Poirel Laurent1,Rodríguez-Martínez Jose-Manuel1,Al Naiemi Nashwan2,Debets-Ossenkopp Yvette J.2,Nordmann Patrice1

Affiliation:

1. Service de Bactériologie-Virologie, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine Paris-Sud, Université Paris XI, Le Kremlin-Bicêtre, France

2. Department of Microbiology, Vrije Universiteit Medical Center, Amsterdam, Netherlands

Abstract

ABSTRACT A carbapenem-resistant Pseudomonas stutzeri strain isolated from a Dutch patient was analyzed in detail. This isolate produced a metallo-β-lactamase (MBL) whose gene, with 43.5% GC content, was cloned and expressed in Escherichia coli. β-Lactamase DIM-1 (for D utch im ipenemase) was weakly related to other Ambler class B β-lactamases, sharing <52% amino acid identity with the most closely related MBL, GIM-1, and 45% identity with IMP-type MBLs. The β-Lactamase DIM-1 significantly hydrolyzed broad-spectrum cephalosporins and carbapenems and spared aztreonam. This MBL gene was embedded in a class 1 integron containing two other gene cassettes, encoding resistance to aminoglycosides and disinfectants, that was located on a 70-kb plasmid.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

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