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
-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
-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
-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]