Previous Article | Next Article ![]()
Antimicrobial Agents and Chemotherapy, November 2005, p. 4443-4447, Vol. 49, No. 11
0066-4804/05/$08.00+0 doi:10.1128/AAC.49.11.4443-4447.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Faculté de Médecine, Centre Hospitalo-Universitaire, Clermont-Ferrand, France
Received 30 March 2005/ Returned for modification 6 June 2005/ Accepted 3 August 2005
Escherichia coli CF349 exhibited a complex ß-lactam resistance phenotype, including resistance to amoxicillin and ticarcillin alone and in combination with clavulanate and to some extended-spectrum cephalosporins. The double-disk synergy test was positive. CF349 harbored an 85-kb conjugative plasmid which encoded a ß-lactamase of pI 5.9. The corresponding bla gene was identified by PCR and sequencing as a blaTEM gene. The deduced protein sequence revealed a new complex mutant of TEM-1 ß-lactamase designated TEM-109 (CMT-5). TEM-109 contained both the substitutions Glu104Lys and Arg164His of the expanded-spectrum ß-lactamase (ESBL) TEM-6 and Met69Leu of the inhibitor-resistant TEM-33 (IRT-5). TEM-109 exhibited hydrolytic activity against ceftazidime similar to that of TEM-6 (kcat, 56 s1 and 105 s1, respectively; Km values, 226 and 247 µM, respectively). The 50% inhibitory concentrations of clavulanate and tazobactam (0.13 µM and 0.27 µM, respectively) were 5- to 10-fold higher for TEM-109 than for TEM-6 (0.01 and 0.06 µM, respectively) but were almost 10-fold lower than those for TEM-33. The characterization of this novel CMT, which exhibits a low level of resistance to inhibitors, highlights the emergence of this new ESBL type.
This paper is devoted to the memory of Catherine Chanal.
This article has been cited by other articles:
| Clin. Vaccine Immunol. | Clin. Microbiol. Rev. |
|---|---|
| J. Clin. Microbiol. | ALL ASM JOURNALS |