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

نویسندگان

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

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.

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عنوان ژورنال:
  • Antimicrobial agents and chemotherapy

دوره 57 10  شماره 

صفحات  -

تاریخ انتشار 2013