This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Poirel, L. Articles by Nordmann, P. Search for Related Content PubMed PubMed Citation Articles by Poirel, L. Articles by Nordmann, P.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, December 2004, p. 4528-4531, Vol. 48, No. 12
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.12.4528-4531.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

TEM-121, a Novel Complex Mutant of TEM-Type ß-Lactamase from Enterobacter aerogenes

Laurent Poirel, Hedi Mammeri, and Patrice Nordmann^*

Service de Bactériologie-Virologie, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine Paris-Sud, Université Paris XI, Le Kremlin-Bicêtre, France

Received 31 March 2004/ Returned for modification 31 May 2004/ Accepted 29 August 2004

Enterobacter aerogenes clinical isolate LOR was resistant to penicillins and ceftazidime but susceptible to cefuroxime, cephalothin, cefoxitin, cefotaxime, ceftriaxone, and cefepime. PCR and cloning experiments from this strain identified a novel TEM-type ß-lactamase (TEM-121) differing by five amino acid substitutions from ß-lactamase TEM-2 (Glu104Lys, Arg164Ser, Ala237Thr, Glu240Lys, and Arg244Ser) and by only one amino acid change from the extended-spectrum ß-lactamase (ESBL) TEM-24 (Arg244Ser), with the last substitution also being identified in the inhibitor-resistant ß-lactamase IRT-2. Kinetic parameters indicated that TEM-121 hydrolyzed ceftazidime and aztreonam (like TEM-24) and was inhibited weakly by clavulanic acid and strongly by tazobactam. Thus, TEM-121 is a novel complex mutant TEM ß-lactamase (CMT-4) combining the kinetic properties of an ESBL and an inhibitor-resistant TEM enzyme.

L.P. and H.M. contributed equally to this work.

This article has been cited by other articles:

• Robin, F., Delmas, J., Brebion, A., Dubois, D., Constantin, J.-M., Bonnet, R. (2007). TEM-158 (CMT-9), a New Member of the CMT-Type Extended-Spectrum {beta}-Lactamases. Antimicrob. Agents Chemother. 51: 4181-4183 [Abstract] [Full Text]  
• Nomura, R., Hamada, M., Nakano, K., Nemoto, H., Fujimoto, K., Ooshima, T. (2007). Repeated bacteraemia caused by Streptococcus mutans in a patient with Sjogren's syndrome. J Med Microbiol 56: 988-992 [Abstract] [Full Text]  
• Robin, F., Delmas, J., Schweitzer, C., Tournilhac, O., Lesens, O., Chanal, C., Bonnet, R. (2007). Evolution of TEM-Type Enzymes: Biochemical and Genetic Characterization of Two New Complex Mutant TEM Enzymes, TEM-151 and TEM-152, from a Single Patient. Antimicrob. Agents Chemother. 51: 1304-1309 [Abstract] [Full Text]  
• Robin, F., Delmas, J., Archambaud, M., Schweitzer, C., Chanal, C., Bonnet, R. (2006). CMT-Type {beta}-Lactamase TEM-125, an Emerging Problem for Extended-Spectrum {beta}-Lactamase Detection.. Antimicrob. Agents Chemother. 50: 2403-2408 [Abstract] [Full Text]  
• Robin, F., Delmas, J., Chanal, C., Sirot, D., Sirot, J., Bonnet, R. (2005). TEM-109 (CMT-5), a Natural Complex Mutant of TEM-1 {beta}-Lactamase Combining the Amino Acid Substitutions of TEM-6 and TEM-33 (IRT-5). Antimicrob. Agents Chemother. 49: 4443-4447 [Abstract] [Full Text]  
• Paterson, D. L., Bonomo, R. A. (2005). Extended-Spectrum {beta}-Lactamases: a Clinical Update. Clin. Microbiol. Rev. 18: 657-686 [Abstract] [Full Text]