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

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, December 2001, p. 3591-3594, Vol. 45, No. 12
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.12.3591-3594.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

TEM-89 beta -Lactamase Produced by a Proteus mirabilis Clinical Isolate: New Complex Mutant (CMT 3) with Mutations in both TEM-59 (IRT-17) and TEM-3

Catherine Neuwirth,1,* Stephanie Madec,2 Eliane Siebor,1 Andre Pechinot,1 Jean-Marie Duez,1 Michele Pruneaux,1 Martine Fouchereau-Peron,2 Antoine Kazmierczak,1 and Roger Labia2

Laboratoire de Bactériologie, Hôpital Universitaire du Bocage, 21034 Dijon Cedex,1 and Unité FRE 2125, CNRS, UBO, MNHN, 29000 Quimper,2 France

Received 20 February 2001/Returned for modification 29 May 2001/Accepted 28 August 2001

TEM-89 (CMT-3) is the first complex mutant beta -lactamase produced by a clinical strain of Proteus mirabilis (strain Pm 631). This new enzyme, which has a pI of 6.28, is derived from TEM-3 and has a single amino acid substitution also encountered in TEM-59 (inhibitor-resistant TEM beta -lactamase IRT-17): Ser-130 to Gly. TEM-89 hydrolyzed penicillins to the same extent that TEM-3 did but lost almost all hydrolytic activity for cephalosporins and, like TEM-59, was highly resistant to inhibitors.

* Corresponding author. Mailing address: Laboratoire de Bactériologie, Hôpital Universitaire du Bocage, BP 1542, 21034 Dijon Cedex, France. Phone: 33-3 80 29 32 60. Fax: 33-3 80 29 36 67. E-mail: catherine.neuwirth{at}chu-dijon.fr.

Antimicrobial Agents and Chemotherapy, December 2001, p. 3591-3594, Vol. 45, No. 12
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.12.3591-3594.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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]  
  • 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]  
  • Poirel, L., Mammeri, H., Nordmann, P. (2004). TEM-121, a Novel Complex Mutant of TEM-Type {beta}-Lactamase from Enterobacter aerogenes. Antimicrob. Agents Chemother. 48: 4528-4531 [Abstract] [Full Text]  
  • Aumeran, C., Chanal, C., Labia, R., Sirot, D., Sirot, J., Bonnet, R. (2003). Effects of Ser130Gly and Asp240Lys Substitutions in Extended-Spectrum {beta}-Lactamase CTX-M-9. Antimicrob. Agents Chemother. 47: 2958-2961 [Abstract] [Full Text]  
  • Galan, J.-C., Morosini, M.-I., Baquero, M.-R., Reig, M., Baquero, F. (2003). Haemophilus influenzae blaROB-1 Mutations in Hypermutagenic {Delta}ampC Escherichia coli Conferring Resistance to Cefotaxime and {beta}-Lactamase Inhibitors and Increased Susceptibility to Cefaclor. Antimicrob. Agents Chemother. 47: 2551-2557 [Abstract] [Full Text]  
  • Schroeder, W. A., Locke, T. R., Jensen, S. E. (2002). Resistance to {beta}-Lactamase Inhibitor Protein Does Not Parallel Resistance to Clavulanic Acid in TEM {beta}-Lactamase Mutants. Antimicrob. Agents Chemother. 46: 3568-3573 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»