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Antimicrobial Agents and Chemotherapy, November 2000, p. 3061-3068, Vol. 44, No. 11
0066-4804/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

A Novel Class A Extended-Spectrum beta -Lactamase (BES-1) in Serratia marcescens Isolated in Brazil

R. Bonnet,1,* J. L. M. Sampaio,2 C. Chanal,1 D. Sirot,1 C. De Champs,1 J. L. Viallard,3 R. Labia,4 and J. Sirot1

Laboratoire de Bactériologie,1 and Laboratoire de Biochimie,3 Faculté de Médecine, 63001 Clermont-Ferrand Cedex, and CNRS-UBO-MNHN, FRE 2125, 29000 Quimper,4 France, and Setor de Bacteriologia, Laboratório Lâmina LTDA, 71-Botafogo, Rio de Janeiro, RJ, Brazil 22280-0302

Received 13 April 2000/Returned for modification 19 July 2000/Accepted 24 August 2000

Serratia marcescens Rio-5, one of 18 extended-spectrum beta -lactamase (ESBL)-producing strains isolated in several hospitals in Rio de Janeiro (Brazil) in 1996 and 1997, exhibited a high level of resistance to aztreonam (MIC, 512 µg/ml) and a distinctly higher level of resistance to cefotaxime (MIC, 64 µg/ml) than to ceftazidime (MIC, 8 µg/ml). The strain produced a plasmid-encoded ESBL with a pI of 7.5 whose bla gene was not related to those of other plasmid-mediated Ambler class A ESBLs. Cloning and sequencing revealed a bla gene encoding a novel class A beta -lactamase in functional group 2be, designated BES-1 (Brazil extended-spectrum beta -lactamase). This enzyme had 51% identity with chromosomal class A penicillinase of Yersinia enterocolitica Y56, which was the most closely related enzyme and 47 to 48% identity with CTX-M-type beta -lactamases, which were the most closely related ESBLs. In common with CTX-M enzymes, BES-1 exhibited high cefotaxime-hydrolyzing activity (kcat, 425 s-1). However, BES-1 differed from CTX-M enzymes by its significant ceftazidime-hydrolyzing activity (kcat, 25 s-1), high affinity for aztreonam (Ki, 1 µM), and lower susceptibility to tazobactam (50% inhibitory concentration [IC50], 0.820 µM) than to clavulanate (IC50, 0.045 µM). Likewise, certain characteristic structural features of CTX-M enzymes, such as Phe-160, Ser-237, and Arg-276, were observed for BES-1, which, in addition, harbored different residues (Ala-104, Ser-171, Arg-220, Gly-240) and six additional residues at the end of the sequence. BES-1, therefore, may be an interesting model for further investigations of the structure-function relationships of class A ESBLs.

* Corresponding author. Mailing address: Faculté de Médecine, Service de Bactériologie-Virologie, 28, Place Henri Dunant, 63001 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 2000, p. 3061-3068, Vol. 44, No. 11
0066-4804/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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