Article (Scientific journals)
Functional diversity among metallo-β-lactamases: Characterization of the CAR-1 enzyme of Erwinia carotovora
Stoczko, M.; Frère, Jean-Marie; Rossolini, G. M. et al.
2008In Antimicrobial Agents and Chemotherapy, 52 (7), p. 2473-2479
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Keywords :
Enterobacteriaceae; Enterobacteriales; Escherichia coli; Pectobacterium carotovorum; Amino Acid Sequence; Bacterial Proteins; Base Sequence; Cloning, Molecular; DNA Primers; DNA, Bacterial; Drug Resistance, Bacterial; Genes, Bacterial; Molecular Sequence Data; Open Reading Frames; Phenotype; Phylogeny; Recombinant Proteins; Sequence Homology, Amino Acid
Abstract :
[en] Metallo-β-lactamases (MBLs) are zinc-dependent bacterial enzymes characterized by an efficient hydrolysis of carbapenems and a lack of sensitivity to commercially available β-lactamase inactivators. Apart from the acquired subclass B1 enzymes, which exhibit increasing clinical importance and whose evolutionary origin remains unclear, most MBLs are encoded by resident genes found in the genomes of organisms belonging to at least three distinct phyla. Using genome database mining, we identified an open reading frame (ORF) (ECA2849) encoding an MBL-like protein in the sequenced genome of Erwinia carotovora, an important plant pathogen. Although no detectable β-lactamase activity could be found in E. carotovora, a recombinant Escherichia coli strain in which the ECA2849 ORF was cloned showed decreased susceptibility to several β-lactams, while carbapenem MICs were surprisingly poorly affected. The enzyme, named CAR-1, was purified by means of ion-exchange chromatography steps, and its characterization revealed unique structural and functional features. This new MBL was able to efficiently hydrolyze cephalothin, cefuroxime, and cefotaxime and, to a lesser extent, penicillins and the other cephalosporins but only poorly hydrolyzed meropenem, while imipenem was not recognized. CAR-1 is the first example of a functional naturally occurring MBL in the family Enterobacteriaceae (order Enterobacteriales) and highlights the extraordinary structural and functional diversity exhibited by MBLs. Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Disciplines :
Biochemistry, biophysics & molecular biology
Microbiology
Author, co-author :
Stoczko, M.;  Dipartimento di Biologia Molecolare, Laboratorio di Fisiologia e Biotecnologia dei Microrganismi, Università di Siena, I-53100, Siena, Italy
Frère, Jean-Marie ;  Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques
Rossolini, G. M.;  Dipartimento di Biologia Molecolare, Laboratorio di Fisiologia e Biotecnologia dei Microrganismi, Università di Siena, I-53100, Siena, Italy
Docquier, Jean-Denis ;  Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines
Language :
English
Title :
Functional diversity among metallo-β-lactamases: Characterization of the CAR-1 enzyme of Erwinia carotovora
Publication date :
2008
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
Volume :
52
Issue :
7
Pages :
2473-2479
Peer reviewed :
Peer Reviewed verified by ORBi
Name of the research project :
HPRN-CT-2002-00264; LSHN-CT-2003-503335
Available on ORBi :
since 23 November 2020

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