Molecular characterization of FOX-4, a new AmpC-type plasmid-mediated beta-lactamase from an Escherichia coli strain isolated in Spain

Antimicrob Agents Chemother. 2000 Sep;44(9):2549-53. doi: 10.1128/AAC.44.9.2549-2553.2000.

Abstract

A clinical strain of Escherichia coli (Ec GCE) displayed resistance to cefoxitin, cefotetan, cefotaxime, and ceftazidime. Susceptibility was not restored by the addition of clavulanic acid. Two beta-lactamases with apparent pIs of 5.4 and 6.4 were identified; the beta-lactamase with a pI of 6.4 was transferred by conjugation and associated with a 40-kb plasmid. Analysis of the nucleotide sequence showed a new ampC beta-lactamase gene that is closely related to those encoding the FOX-3, FOX-2, and FOX-1 beta-lactamases but whose product has four novel amino acid mutations, at positions 11 (M-->T), 43 (A-->E), 233 (V-->A), and 280 (Y-->H). This first cephamycinase from Spain was named FOX-4.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins*
  • Base Sequence
  • Cloning, Molecular
  • DNA, Bacterial / analysis
  • Drug Resistance, Microbial / genetics
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology
  • Escherichia coli / genetics*
  • Escherichia coli Proteins
  • Humans
  • Hydrolysis
  • Isoelectric Focusing
  • Kinetics
  • Molecular Sequence Data
  • Plasmids / genetics
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Spanien
  • beta-Lactamases / chemistry
  • beta-Lactamases / drug effects
  • beta-Lactamases / genetics*
  • beta-Lactams

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • DNA, Bacterial
  • Escherichia coli Proteins
  • beta-Lactams
  • fox-4 protein, E coli
  • AmpC beta-lactamases
  • beta-Lactamases

Associated data

  • GENBANK/AJ277535