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

doi:10.1128/AAC.00818-13

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

Department of Genetics and Microbiology

Research output: Contribution to journal › Article › Research › peer-review

7 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 language	English
Pages (from-to)	5158-5161
Journal	Antimicrobial Agents and Chemotherapy
Volume	57
Issue number	10
DOIs	https://doi.org/10.1128/AAC.00818-13
Publication status	Published - 1 Oct 2013

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Pérez-Llarena, F. J., Kerff, F., Zamorano, L., Fernández, M. C., Nuñez, M. L., Miró, E., Oliver, A., Navarro, F., & Bou, G. (2013). Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 Loop that affects ceftazidime hydrolysis. Antimicrobial Agents and Chemotherapy, 57(10), 5158-5161. https://doi.org/10.1128/AAC.00818-13

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

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 {\textcopyright} 2013, American Society for Microbiology. All Rights Reserved.",

author = "P{\'e}rez-Llarena, {Francisco Jos{\'e}} and Fr{\'e}d{\'e}ric Kerff and Laura Zamorano and Fern{\'a}ndez, {Mar{\'i}a Carmen} and Nu{\~n}ez, {Maria Luz} and Elisenda Mir{\'o} and Antonio Oliver and Ferran Navarro and Germ{\'a}n Bou",

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doi = "10.1128/AAC.00818-13",

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Pérez-Llarena, FJ, Kerff, F, Zamorano, L, Fernández, MC, Nuñez, ML, Miró, E, Oliver, A, Navarro, F & Bou, G 2013, 'Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 Loop that affects ceftazidime hydrolysis', Antimicrobial Agents and Chemotherapy, vol. 57, no. 10, pp. 5158-5161. https://doi.org/10.1128/AAC.00818-13

Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 Loop that affects ceftazidime hydrolysis. / Pérez-Llarena, Francisco José; Kerff, Frédéric; Zamorano, Laura et al.
In: Antimicrobial Agents and Chemotherapy, Vol. 57, No. 10, 01.10.2013, p. 5158-5161.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 Loop that affects ceftazidime hydrolysis

AU - Pérez-Llarena, Francisco José

AU - Kerff, Frédéric

AU - Zamorano, Laura

AU - Fernández, María Carmen

AU - Nuñez, Maria Luz

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AU - Oliver, Antonio

AU - Navarro, Ferran

AU - Bou, Germán

PY - 2013/10/1

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AB - 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.

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DO - 10.1128/AAC.00818-13

M3 - Article

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ER -

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

Abstract

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