Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 Loop that affects ceftazidime hydrolysis

Francisco José Pérez-Llarena, Frédéric Kerff, Laura Zamorano, María Carmen Fernández, Maria Luz Nuñez, Elisenda Miró, Antonio Oliver, Ferran Navarro, Germán Bou

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4 Citations (Scopus)

Abstract

A novel class C β-lactamase (FOX-8) was isolated from a clinical strain of Escherichia coli. The FOX-8 enzyme possessed a unique substitution (Phe313Leu) compared to FOX-3. Isogenic E. coli strains carrying FOX-8 showed an 8-fold reduction in resistance to ceftazidime relative to FOX-3. In a kinetic analysis, FOX-8 displayed a 33-fold reduction in kcat/Km for ceftazidime compared to FOX-3. In the FOX family of β-lactamases, the Phe313 residue located in the R2 loop affects ceftazidime hydrolysis and alters the phenotype of E. coli strains carrying this variant. Copyright © 2013, American Society for Microbiology. All Rights Reserved.
Original languageEnglish
Pages (from-to)5158-5161
JournalAntimicrobial Agents and Chemotherapy
Volume57
Issue number10
DOIs
Publication statusPublished - 1 Oct 2013

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