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Antimicrobial Agents and Chemotherapy, September 1999, p. 2193-2199, Vol. 43, No. 9
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Cloning of a Chryseobacterium (Flavobacterium) meningosepticum Chromosomal Gene (blaACME) Encoding an Extended-Spectrum Class A beta -Lactamase Related to the Bacteroides Cephalosporinases and the VEB-1 and PER beta -Lactamases

Gian Maria Rossolini,1,* Nicola Franceschini,2 Laura Lauretti,1 Berardo Caravelli,2 Maria Letizia Riccio,1 Moreno Galleni,3 Jean-Marie Frère,3 and Gianfranco Amicosante2

Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Università degli Studi di Siena, 53100 Siena,1 and Dipartimento di Scienze e Tecnologie Biomediche e di Biometria, Cattedra di Chimica Biologica, Università degli Studi dell'Aquila, 67100 Coppito, L'Aquila,2 Italy, and Centre d'Ingénierie des Protéines, Université de Liège, Sart Tilman, B-4000 Liège, Belgium3

Received 15 January 1999/Returned for modification 26 April 1999/Accepted 25 June 1999

In addition to the BlaB metallo-beta -lactamase, Chryseobacterium (Flavobacterium) meningosepticum CCUG 4310 (NCTC 10585) constitutively produces a 31-kDa active-site serine beta -lactamase, named CME-1, with an alkaline isoelectric pH. The blaACME gene that encodes the latter enzyme was isolated from a genomic library constructed in the Escherichia coli plasmid vector pACYC184 by screening for cefuroxime-resistant clones. Sequence analysis revealed that the CME-1 enzyme is a new class A beta -lactamase structurally divergent from the other members of this class, being most closely related to the VEB-1 (also named CEF-1) and PER beta -lactamases and the Bacteroides chromosomal cephalosporinases. The blaACME determinant is located on the chromosome and exhibits features typical of those of C. meningosepticum resident genes. The CME-1 protein was purified from an E. coli strain that overexpresses the cloned gene via a T7-based expression system by means of an anion-exchange chromatography step followed by a gel permeation chromatography step. Kinetic parameters for several substrates were determined. CME-1 is a clavulanic acid-susceptible extended-spectrum beta -lactamase that hydrolyzes most cephalosporins, penicillins, and monobactams but that does not hydrolyze cephamycins and carbapenems. The enzyme exhibits strikingly different kinetic parameters for different classes of beta -lactams, with both Km and kcat values much higher for cephalosporins than for penicillins and monobactams. However, the variability of both kinetic parameters resulted in overall similar acylation rates (kcat/Km ratios) for all types of beta -lactam substrates.

* Corresponding author. Mailing address: Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Università degli Studi di Siena, Via Laterina, 8, 53100 Siena, Italy. Phone: 39 0577 233455. Fax: 39 0577 233325. E-mail: rossolini{at}unisi.it.

Antimicrobial Agents and Chemotherapy, September 1999, p. 2193-2199, Vol. 43, No. 9
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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