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Antimicrobial Agents and Chemotherapy, February 1999, p. 297-301, Vol. 43, No. 2
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization and Nucleotide Sequence of CARB-6, a New Carbenicillin-Hydrolyzing beta -Lactamase from Vibrio cholerae

Danièle Choury,1,* Gérald Aubert,2 Marie-France Szajnert,3 Kemal Azibi,3,4 Marc Delpech,1 and Gérard Paul5

Laboratoire de Biologie Moléculaire des Cellules Eucaryotes,1 INSERM U129,3 and Laboratoire de Recherche en Microbiologie,5 UFR Cochin Port-Royal, 75014 Paris, and Laboratoire de Bactériologie, CHU, Saint-Etienne,2 France, and CHU Alger-Ouest, Algiers, Algeria4

Received 28 May 1998/Returned for modification 21 September 1998/Accepted 20 November 1998

A clinical strain of Vibrio cholerae non-O1 non-O139 isolated in France produced a new beta -lactamase with a pI of 5.35. The purified enzyme, with a molecular mass of 33,000 Da, was characterized. Its kinetic constants show it to be a carbenicillin-hydrolyzing enzyme comparable to the five previously reported CARB beta -lactamases and to SAR-1, another carbenicillin-hydrolyzing beta -lactamase that has a pI of 4.9 and that is produced by a V. cholerae strain from Tanzania. This beta -lactamase is designated CARB-6, and the gene for CARB-6 could not be transferred to Escherichia coli K-12 by conjugation. The nucleotide sequence of the structural gene was determined by direct sequencing of PCR-generated fragments from plasmid DNA with four pairs of primers covering the whole sequence of the reference CARB-3 gene. The gene encodes a 288-amino-acid protein that shares 94% homology with the CARB-1, CARB-2, and CARB-3 enzymes, 93% homology with the Proteus mirabilis N29 enzyme, and 86.5% homology with the CARB-4 enzyme. The sequence of CARB-6 differs from those of CARB-3, CARB-2, CARB-1, N29, and CARB-4 at 15, 16, 17, 19, and 37 amino acid positions, respectively. All these mutations are located in the C-terminal region of the sequence and at the surface of the molecule, according to the crystal structure of the Staphylococcus aureus PC-1 beta -lactamase.

* Corresponding author. Mailing address: Laboratoire de Biologie Moléculaire des Cellules Eucaryotes, UFR Cochin Port-Royal, 24 rue du Faubourg Saint-Jacques, 75014 Paris, France. Phone: 00 33 1 44 41 23 47. Fax: 00 33 1 44 41 23 42. E-mail: paul{at}citi2.fr.

Antimicrobial Agents and Chemotherapy, February 1999, p. 297-301, Vol. 43, No. 2
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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