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Antimicrobial Agents and Chemotherapy, June 2002, p. 1823-1830, Vol. 46, No. 6
0066-4804/02/$04.00+0     DOI: 10.1128/AAC.46.6.1823-1830.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

CAU-1, a Subclass B3 Metallo-ß-Lactamase of Low Substrate Affinity Encoded by an Ortholog Present in the Caulobacter crescentus Chromosome

Jean-Denis Docquier,1 Fabrizio Pantanella,2 Francesco Giuliani,1 Maria Cristina Thaller,3 Gianfranco Amicosante,4 Moreno Galleni,5 Jean-Marie Frère,5 Karen Bush,6 and Gian Maria Rossolini1*

Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Università di Siena, 53100 Siena,1 Dipartimento di Sanità Pubblica, Sezione di Microbiologia, Università di Roma "La Sapienza," 00185 Rome,2 Dipartimento di Biologia, Università di Roma "Tor Vergata," 00133 Rome,3 Dipartimento di Scienze e Tecnologie Biomediche, Università di L'Aquila, 67100 L'Aquila, Italy,4 Laboratoire d'Enzymologie et Centre d'Ingénierie des Protéines, Institut de Chimie, Université de Liège, Sart Tilman, B-4000 Liège, Belgium,5 RW Johnson Pharmaceutical Research Institute, Raritan, New Jersey6

Received 15 October 2001/ Returned for modification 3 January 2002/ Accepted 10 March 2002

The sequenced chromosome of Caulobacter crescentus CB15 encodes a hypothetical protein that exhibits significant similarity (30 to 35% identical residues) to metallo-ß-lactamases of subclass B3. An allelic variant of this gene (divergent by 3% of its nucleotides) was cloned in Escherichia coli from C. crescentus type strain DSM4727. Expression studies confirmed the metallo-ß-lactamase activity of its product, CAU-1. The enzyme produced in E. coli was purified by two ion-exchange chromatography steps. CAU-1 contains a 29-kDa polypeptide with an alkaline isoelectric pH (>9), and unlike the L1 enzyme of Stenotrophomonas maltophilia, the native form is monomeric. Kinetic analysis revealed a preferential activity toward penicillins, carbapenems, and narrow-spectrum cephalosporins, while oxyimino cephalosporins were poorly or not hydrolyzed. Affinities for the various ß-lactams were poor overall (Km values were always >100 µM and often >400 µM). The interaction with divalent ion chelators appeared to occur by a mechanism similar to that prevailing in other members of subclass B3. In C. crescentus, the CAU-1 enzyme is produced independently of ß-lactam exposure and, interestingly, the blaCAU determinant is bracketed by three other genes, including two genes encoding enzymes involved in methionine biosynthesis and a gene encoding a putative transcriptional regulator, in an operon-like structure. The CAU-1 enzyme is the first example of a metallo-ß-lactamase in a member of the {alpha} subdivision of the class Proteobacteria.

* Corresponding author. Mailing address: Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Università di Siena, Policlinico Le Scotte, 53100 Siena, Italy. Phone: 39 0577 233327. Fax: 39 0577 233325. E-mail: rossolini{at}unisi.it.

Antimicrobial Agents and Chemotherapy, June 2002, p. 1823-1830, Vol. 46, No. 6
0066-4804/02/$04.00+0     DOI: 10.1128/AAC.46.6.1823-1830.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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