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Antimicrobial Agents and Chemotherapy, July 2006, p. 2403-2408, Vol. 50, No. 7
0066-4804/06/$08.00+0 doi:10.1128/AAC.01639-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
CHU Clermont-Ferrand, Laboratoire de Bactériologie,1 Université Clermont 1, EA3844, Faculté de Médecine-Pharmacie, Clermont-Ferrand,2 CHU Toulouse, Hôpital Rangueil, Laboratoire de Bactériologie, Toulouse, France3
Received 26 December 2005/ Returned for modification 8 March 2006/ Accepted 13 April 2006
The clinical strain Escherichia coli TO799 was resistant to penicillin-clavulanate combinations and ceftazidime and was not reproducibly detected as an extended-spectrum ß-lactamase (ESBL) according to the standards of the Clinical Laboratory Standards Institute (CLSI; formerly NCCLS) and the national guidelines of the French Society for Microbiology (Comité de l'Antibiogramme de la Société Française de Microbiologie). A novel ß-lactamase, designated TEM-125, was responsible for this phenotype. TEM-125 harbors a complex association of mutations previously described in the ESBL TEM-12 and in the inhibitor-resistant ß-lactamase TEM-39. TEM-125 is the first complex mutant TEM to present hydrolytic activity against ceftazidime (kcat, 3.7 s1) together with a high level of resistance to clavulanate (50% inhibitory concentration, 13.6 µM). The discovery of such an ESBL, which is difficult to detect by the usual ESBL detection methods, confirms the emergence of a complex mutant TEM subgroup and highlights the need to evaluate detection methods so as to avoid possible therapeutic failures.
This work is dedicated to the memory of Catherine Chanal.
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