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Antimicrobial Agents and Chemotherapy, August 2006, p. 2673-2679, Vol. 50, No. 8
0066-4804/06/$08.00+0     doi:10.1128/AAC.00058-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Genetic and Biochemical Characterization of FUS-1 (OXA-85), a Narrow-Spectrum Class D ß-Lactamase from Fusobacterium nucleatum subsp. polymorphum

Christine Voha,1 Jean-Denis Docquier,2,3 Gian Maria Rossolini,3 and Thierry Fosse1*

Laboratoire de Bactériologie et Epidémiologie Moléculaire, Université de Nice, Centre Hospitalier Universitaire de Nice, F-06202 Nice, France,1 Centre d'Ingénierie des Protéines et Laboratoire d'Enzymologie, Université de Liège, B-4000 Sart-Tilman, Belgium,2 Dipartimento di Biologia Molecolare, Laboratorio di Fisiologia e Biotecnologia dei Microrganismi, Università di Siena, I-53100 Siena, Italy3

Received 13 January 2006/ Returned for modification 8 March 2006/ Accepted 26 May 2006

Previous studies have reported ß-lactamase-mediated penicillin resistance in Fusobacterium nucleatum, but no ß-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 ß-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 blaFUS-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 ß-lactamase gene. The FUS-1 enzyme showed the closest ancestral relationship with OXA-63 from Brachyspira pilosicoli (53% identity) and with putative chromosomal ß-lactamases of Campylobacter spp. (40 to 42% identity). FUS-1 presents all of the conserved structural motifs of class D ß-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 NaCl. FUS-1 is the first example of a class D ß-lactamase produced by a gram-negative, anaerobic, rod-shaped bacterium to be characterized.

* Corresponding author. Mailing address: Laboratoire de bactériologie, 151 route de St Antoine de Ginestière, Hôpital Archet, 06202 Nice Cédex 03, France. Phone: (33) 492036212. Fax: (33) 492036549. E-mail: fosse{at}unice.fr.

Antimicrobial Agents and Chemotherapy, August 2006, p. 2673-2679, Vol. 50, No. 8
0066-4804/06/$08.00+0     doi:10.1128/AAC.00058-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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