AAC Accepts, published online ahead of print on 16 June 2008

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Antimicrob. Agents Chemother. doi:10.1128/AAC.00166-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Kinetic Characterization of VIM-7, A Divergent Member of the VIM Metallo--Lactamase-Family

rjan Samuelsen^*, Mariana Castanheira, Timothy R. Walsh, and James Spencer^*

Reference Centre for Detection of Antimicrobial Resistance, Department of Microbiology and Infection Control, University Hospital of North Norway, Tromsø, Norway; Department of Cellular and Molecular Medicine, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD, UK; Department of Medical Microbiology, University of Cardiff, Heath Park, Cardiff CF14 4XN, UK; JMI Laboratories, North Liberty, IA 52317, USA

^* To whom correspondence should be addressed. Email: orjan.samuelsen{at}unn.no. Jim.Spencer{at}bristol.ac.uk.

Purified recombinant VIM-7 possesses efficient penicillinase and carbapenemase activity comparable to VIM-2. Cephalosporinase activity was variable and generally lower than for VIM-1 or VIM-2. An homology model suggests that the VIM-7 Tyr-218 Phe substitution may be responsible for the reduced catalytic efficiency against certain cephalosporins, including ceftazidime and cefepime.

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