Inhibitor-resistant TEM (IRT) beta-lactamases with different substitutions at position 244

Author:

Bret L1,Chaibi E B1,Chanal-Claris C1,Sirot D1,Labia R1,Sirot J1

Affiliation:

1. Laboratoire de Bactériologie, Faculté de Médecine, Clermont-Ferrand, France.

Abstract

A novel inhibitor-resistant TEM (IRT) beta-lactamase was detected in an Escherichia coli isolate resistant to amoxicillin-clavulanate and susceptible to cephalothin. The substrate and inhibitor profiles of this beta-lactamase were similar to those of IRT-1 and IRT-2. The novel IRT's bla gene was sequenced, and the deduced amino acid sequence showed the amino acid replacement Arg for His-244 of the TEM-1 sequence. Substitutions for Arg-244 have been reported in three TEM-1 mutants: IRT-1 (which corresponds to TEM-31) (Cys), IRT-2/TEM-30 (Ser), and TEM-41 (Thr). We designated this novel beta-lactamase, which corresponds to TEM-51, IRT-15.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Reference23 articles.

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2. Nucleotide sequences of the genes coding for the TEM-like ~-lactamases IRT-1 and IRT-2 (formerly called TRI-1 and TRI-2);Belaaouaj A.;FEMS Microbiol. Lett.,1994

3. Characterization of a new TEM-type ~-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli;Blazquez J.;Antimicrob. Agents Chemother.,1993

4. Characterization of an inhibitor-resistant enzyme IRT-2 derived from TEM-2 ~-lactamase produced by Proteus mirabilis strains;Bret L.;J. Antimicrob. Chemother.,1996

5. Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to ~-lactamase inhibitors;Brun T.;FEMS Microbiol. Lett.,1994

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