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Antimicrobial Agents and Chemotherapy, February 2001, p. 546-552, Vol. 45, No. 2
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.2.546-552.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of Class 1 Integrons from Pseudomonas aeruginosa That Contain the blaVIM-2 Carbapenem-Hydrolyzing beta -Lactamase Gene and of Two Novel Aminoglycoside Resistance Gene Cassettes

Laurent Poirel,1 Thierry Lambert,2 Salih Türkoglü,1,3 Esthel Ronco,4 Jean-Louis Gaillard,4 and Patrice Nordmann1,*

Service de Bactériologie-Virologie, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine Paris-Sud, 94275 Le Kremlin-Bicêtre,1 Centre d'Etudes Pharmaceutiques, 92296 Châtenay-Malabry,2 and Service de Microbiologie, Hôpital Raymond Poincaré, Assistance Publique Hôpitaux de Paris, Faculté de Médecine Paris-Ouest, 92380 Garches,4 France, and Department of Virology and Immunology, Istanbul Faculty of Medicine, 34390 Capa Istanbul, Turkey3

Received 19 May 2000/Returned for modification 24 August 2000/Accepted 17 November 2000

Two clonally unrelated Pseudomonas aeruginosa clinical strains, RON-1 and RON-2, were isolated in 1997 and 1998 from patients hospitalized in a suburb of Paris, France. Both isolates expressed the class B carbapenem-hydrolyzing beta -lactamase VIM-2 previously identified in Marseilles in the French Riviera. In both isolates, the blaVIM-2 cassette was part of a class 1 integron that also encoded aminoglycoside-modifying enzymes. In one case, two novel aminoglycoside resistance gene cassettes, aacA29a and aacA29b, were located at the 5' and 3' end of the blaVIM-2 gene cassette, respectively. The aacA29a and aacA29b gene cassettes were fused upstream with a 101-bp part of the 5' end of the qacE cassette. The deduced amino acid sequence AAC(6')-29a protein shared 96% identity with AAC(6')-29b but only 34% identity with the aacA7-encoded AAC(6')-I1, the closest relative of the AAC(6')-I family enzymes. These aminoglycoside acetyltransferases had amino acid sequences much shorter (131 amino acids) than the other AAC(6')-I enzymes (144 to 153 amino acids). They conferred resistance to amikacin, isepamicin, kanamycin, and tobramycin but not to gentamicin, netilmicin, and sisomicin.

* Corresponding author. Mailing address: Service de Bactériologie-Virologie, Hôpital de Bicêtre, 78 rue du Général Leclerc, 94275 Le Kremlin-Bicêtre cedex, France. Phone: 33 1 45 21 36 32. Fax: 33 1 45 21 63 40. E-mail: nordmann.patrice{at}bct.ap-hop-paris.fr.

Antimicrobial Agents and Chemotherapy, February 2001, p. 546-552, Vol. 45, No. 2
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.2.546-552.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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