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Antimicrobial Agents and Chemotherapy, December 2004, p. 4654-4661, Vol. 48, No. 12
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.12.4654-4661.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Molecular Characterization of a ß-Lactamase Gene, blaGIM-1, Encoding a New Subclass of Metallo-ß-Lactamase

Mariana Castanheira,1,2* Mark A. Toleman,2 Ronald N. Jones,3 Franz J. Schmidt,4 and Timothy R. Walsh2

Disciplina de Doencas Infecciosas e Parasitarias, Universidade Federal de Sao Paulo, Sao Paulo, Brazil,1 Department of Pathology and Microbiology, University of Bristol, Bristol, United Kingdom,2 The JONES Group/JMI Laboratories, North Liberty, Iowa,3 Institut fur Laboratoriumsmedizin, Mikrobiologie, Minden, Germany4

Received 17 February 2004/ Returned for modification 1 May 2004/ Accepted 16 August 2004

As part of the SENTRY Antimicrobial Surveillance Program in 2002, five multidrug-resistant Pseudomonas aeruginosa clinical isolates were detected with metallo-ß-lactamase (MßL) activity. The isolates were recovered from different patients in a medical center located in Dusseldorf, Germany. The resistant determinant was isolated amplifying the region between the integrase and the aacA4 gene cassette. Sequencing revealed a novel MßL gene, designated blaGIM-1. Additional analysis showed that GIM-1, comprising 250 amino acids and with a pI value of 5.4, differs in its primary sequence from that described for IMP, VIM, and SPM-1 enzymes by 39 to 43%, 28 to 31%, and 28%, respectively. The enzyme possesses unique amino acids within the major consensus sequence (HXHXD) of the MßL family. Kinetics analysis revealed that GIM-1 has no clear preference for any substrate and did not hydrolyze azlocillin, aztreonam, and the serine-ß-lactamase inhibitors. blaGIM-1 was found on a 22-kb nontransferable plasmid. The new MßL gene was embedded in the first position of a 6-kb class 1 integron, In77, with distinct features, including an aacA4 cassette downstream of the MßL gene that appeared to be truncated with blaGIM-1. The aacA4 was followed by an aadA1 gene cassette that was interrupted by a copy of the IS1394. This integron also carried an oxacillinase gene, blaOXA-2, before the 3'-CS region. GIM-1 appears to be a unique MßL, which is located in a distinct integron structure, and represents the fourth subclass of mobile MßL enzymes to be characterized.

* Corresponding author. Mailing address: Department of Pathology and Microbiology, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom. Phone: 44-117-9288819. Fax: 44-117-9287896. E-mail: maricastanh{at}yahoo.com.

Antimicrobial Agents and Chemotherapy, December 2004, p. 4654-4661, Vol. 48, No. 12
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.12.4654-4661.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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