4.7 Article

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

Journal

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 54, Issue 6, Pages 2420-2424

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.01456-09

Keywords

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Funding

  1. INSERM, France
  2. Ministere de l'Education Nationale et de la Recherche [UPRES-EA3539]
  3. Universite Paris XI, France
  4. European Community [LSHM-CT-2005-018705, HEALTH-F3-2008-223031]
  5. Ministerio de Educacion y Ciencia from Spain [2007/0292]

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A carbapenem-resistant Pseudomonas stutzeri strain isolated from a Dutch patient was analyzed in detail. This isolate produced a metallo-beta-lactamase (MBL) whose gene, with 43.5% GC content, was cloned and expressed in Escherichia coli. beta-Lactamase DIM-1 (for Dutch imipenemase) was weakly related to other Ambler class B beta-lactamases, sharing <52% amino acid identity with the most closely related MBL, GIM-1, and 45% identity with IMP-type MBLs. The beta-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.

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