Article (Scientific journals)
Genetic and biochemical characterization of FUS-1 (OXA-85), a narrow-spectrum class D β-lactamase from Fusobacterium nucleatum subsp. polymorphum
Voha, Christine; Docquier, Jean-Denis; Rossolini, G. M. et al.
2006In Antimicrobial Agents and Chemotherapy, 50 (8), p. 2673-2679
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Keywords :
Brachyspira pilosicoli; Campylobacter; DNA sequence; Escherichia coli; Fusobacterium; Fusobacterium nucleatum polymorphum; Gram negative bacterium; Amino Acid Sequence; Amoxicillin; Anti-Bacterial Agents; Base Sequence; Clavulanic Acid; Drug Resistance, Multiple, Bacterial; Fusobacterium nucleatum; Genes, Bacterial; Humans; Kinetics; Microbial Sensitivity Tests; Molecular Sequence Data; Molecular Weight; Open Reading Frames; Penicillins; Phylogeny; Protein Structure, Secondary; Salts; Sequence Homology, Amino Acid; Substrate Specificity
Abstract :
[en] Previous studies have reported β-lactamase-mediated penicillin resistance in Fusobacterium nucleatum, but no β-lactamase gene has yet been identified in this species. An F. nucleatum subsp. polymorphum strain resistant to penicillin and amoxicillin was isolated from a human periodontitis sample. DNA cloning and sequencing revealed a 765-bp open reading frame encoding a new class D β-lactamase named FUS-1 (OXA-85). A recombinant Escherichia coli strain carrying the blaFUS-1 gene exhibited resistance to amoxicillin with a moderate decrease in the MICs with clavulanic acid. The bla FUS-1 gene was found in two additional clonally unrelated F. nucleatum subsp. polymorphum isolates. It was located on the chromosome in a peculiar genetic environment where a gene encoding a putative transposase-like protein is found, suggesting a possible acquisition of this class D β-lactamase gene. The FUS-1 enzyme showed the closest ancestral relationship with OXA-63 from Brachyspira pilosicoli (53% identity) and with putative chromosomal β-lactamases of Campylobacter spp. (40 to 42% identity). FUS-1 presents all of the conserved structural motifs of class D β-lactamases. Kinetic analysis revealed that FUS-1 exhibits a narrow substrate profile, efficiently hydrolyzing benzylpenicillin and oxacillin. FUS-1 was poorly inactivated by clavulanate and NaC1. FUS-1 is the first example of a class D β-lactamase produced by a gram-negative, anaerobic, rod-shaped bacterium to be characterized. Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Disciplines :
Microbiology
Biochemistry, biophysics & molecular biology
Author, co-author :
Voha, Christine;  Laboratoire de Bactériologie et Epidémiologie Moléculaire, Université de Nice, Centre Hospitalier Universitaire de Nice, F-06202 Nice, France
Docquier, Jean-Denis ;  Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines
Rossolini, G. M.;  Dipartimento di Biologia Molecolare, Laboratorio di Fisiologia e Biotecnologia dei Microrganismi, Università di Siena, I-53100 Siena, Italy
Fosse, Thierry;  Laboratoire de Bactériologie et Epidémiologie Moléculaire, Université de Nice, Centre Hospitalier Universitaire de Nice, F-06202 Nice, France, Laboratoire de Bactériologie, Hôpital Archet, 151 rte. de St Antoine de Ginestiere, 06202 Nice Cedex 03, France
Language :
English
Title :
Genetic and biochemical characterization of FUS-1 (OXA-85), a narrow-spectrum class D β-lactamase from Fusobacterium nucleatum subsp. polymorphum
Publication date :
2006
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
Volume :
50
Issue :
8
Pages :
2673-2679
Peer reviewed :
Peer Reviewed verified by ORBi
Name of the research project :
LSHM-CT-2003-503335
Available on ORBi :
since 25 November 2020

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