Characterization of a novel AmpC β-lactamase produced by a carbapenem-resistant Cedecea davisae clinical isolate

Antimicrob Agents Chemother. 2014 Nov;58(11):6942-5. doi: 10.1128/AAC.03237-14. Epub 2014 Aug 18.

Abstract

A Cedecea davisae isolate, which was intermediate or resistant to third-generation cephalosporins and carbapenems, was recovered from a urine sample. Susceptibility testing, isoelectric focusing, and analysis of outer membrane proteins showed that AmpC β-lactamase expression combined with porin deficiency accounted for the carbapenem resistance. A cloning experiment followed by phenotypic and enzymatic characterization identified a novel class C enzyme that was phylogenetically and biochemically close to the chromosome-borne β-lactamases of the genera Enterobacter and Citrobacter.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Proteins / biosynthesis
  • Bacterial Proteins / genetics*
  • Carbapenems / pharmacology*
  • Drug Resistance, Bacterial / genetics
  • Enterobacteriaceae / drug effects*
  • Enterobacteriaceae / enzymology*
  • Enterobacteriaceae / genetics
  • Female
  • Humans
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Phylogeny
  • Porins / genetics
  • beta-Lactamases / biosynthesis
  • beta-Lactamases / genetics*

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Carbapenems
  • Porins
  • AmpC beta-lactamases
  • beta-Lactamases
  • carbapenemase

Associated data

  • GENBANK/KJ650399