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Antimicrobial Agents and Chemotherapy, November 1999, p. 2671-2677, Vol. 43, No. 11
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Diversity of TEM Mutants in Proteus mirabilis

R. Bonnet,1,* C. De Champs,1 D. Sirot,1 C. Chanal,1 R. Labia,2 and J. Sirot1

Laboratoire de Bactériologie, Faculté de Médecine, 63001 Clermont-Ferrand Cedex,1 and UMR 175, CNRS-MNHN, 29000 Quimper,2 France

Received 24 February 1999/Returned for modification 29 June 1999/Accepted 18 August 1999

In a survey of resistance to amoxicillin among clinical isolates of Proteus mirabilis, 10 TEM-type beta -lactamases were characterized: (i) the well-known penicillinases TEM-1 and TEM-2, the extended-spectrum beta -lactamases (ESBLs) TEM-3 and TEM-24, and the inhibitor-resistant TEM (IRT) TEM-44 and (ii) five novel enzymes, a penicillinase TEM-57 similar to TEM-1, an ESBL TEM-66 similar to TEM-3, and three IRTs, TEM-65, TEM-73, and TEM-74. The penicillinase TEM-57 and the ESBL TEM-66 differed from TEM-1 and TEM-3, respectively, by the amino acid substitution Gly-92right-arrowAsp (nucleotide mutation G-477right-arrowA). This substitution could have accounted for the decrease in pIs (5.2 for TEM-57 and 6.0 for TEM-66) but did not necessarily affect the intrinsic activities of these enzymes. The IRT TEM-65 was an IRT-1-like IRT (Cys-244) related to TEM-2 (Lys-39). The two other IRTs, TEM-73 and TEM-74, were related to IRT-1 (Cys-244) and IRT-2 (Ser-244), respectively, and harbored the amino acid substitutions Leu-21right-arrowPhe and Thr-265right-arrowMet. In this study, the ESBLs TEM-66, TEM-24, and TEM-3 were encoded by large (170- to 180-kb) conjugative plasmids that exhibited similar patterns after digestion and hybridization with the TEM and AAC(6')I probes. The three IRTs TEM-65, TEM-73, and TEM-74 were encoded by plasmids that ranged in size from 42 to 70 kb but for which no transfer was obtained. The characterization of five new plasmid-mediated TEM-type beta -lactamases and the first report of TEM-24 in P. mirabilis are evidence of the wide diversity of beta -lactamases produced in this species and of its possible role as a beta -lactamase-encoding plasmid reservoir.

* Corresponding author. Mailing address: Faculté de Médecine, Service de Bactériologie-Virologie, 28, place Henri Dunant, 63 001 Clermont-Ferrand Cedex, France. Phone: 33 (0)4 73 60 80 18. Fax: 33 (0)4 73 27 74 94. E-mail: Richard.Bonnet{at}u-clermont1.fr.

Antimicrobial Agents and Chemotherapy, November 1999, p. 2671-2677, Vol. 43, No. 11
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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