Increased expression levels of chromosomal AmpC β-lactamase in clinical Escherichia coli isolates and their effect on susceptibility to extended-spectrum cephalosporins

Microb Drug Resist. 2015 Feb;21(1):7-16. doi: 10.1089/mdr.2014.0108. Epub 2014 Sep 4.

Abstract

Forty-nine clinical Escherichia coli isolates, both extended-spectrum β-lactamase (ESBL) negative and ESBL positive, were studied to investigate whether increased AmpC expression is a mechanism involved in cefoxitin resistance and if this influences the third-generation cephalosporin activity. Nine of 33 (27.2%) cefoxitin-resistant (minimum inhibitory concentration [MIC] >8 mg/L) isolates showed hyperproduction of chromosomal AmpC (c-AmpC) based on (1) at least two positive tests using AmpC inhibitors, (2) mutations in the promoter/attenuator regions, and (3) a 6.1- to 163-fold increase in c-ampC expression by quantitative reverse transcription-polymerase chain reaction. In ESBL-negative isolates, MICs of ceftazidime and cefotaxime were mostly above the wild-type (WT) level, but below the S/I breakpoint (EUCAST guideline), except for one isolate with MICs of 4 mg/L. No plasmid-mediated AmpCs were found. Periplasmic extracts of nine c-AmpC hyperproducers were preincubated with or without cefuroxime or ceftazidime and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Cefuroxime and ceftazidime were stable to hydrolysis but acted as inhibitors of the enzyme. None of these isolates showed loss of porins. Thus, cefoxitin resistance has low specificity for detecting upregulated c-AmpC production. c-AmpC hyperproducing E. coli is mostly still susceptible to third-generation cephalosporins but less than WT E. coli. Surveillance of cefoxitin-resistant E. coli to monitor developments in the activity of third-generation cephalosporins against c-AmpC hyperproducers is warranted.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacterial Proteins / biosynthesis*
  • Bacterial Proteins / genetics
  • Cephalosporins / metabolism
  • Cephalosporins / pharmacology*
  • Chromosomes, Bacterial / genetics
  • Drug Resistance, Multiple, Bacterial
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli Infections / microbiology*
  • Escherichia coli Proteins / biosynthesis*
  • Escherichia coli Proteins / genetics
  • Gene Expression Regulation, Bacterial
  • Genes, Bacterial
  • Humans
  • Microbial Sensitivity Tests
  • Sequence Alignment
  • Sequence Homology, Nucleic Acid
  • Substrate Specificity
  • beta-Lactamases / biosynthesis*
  • beta-Lactamases / genetics

Substances

  • Anti-Bacterial Agents
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Cephalosporins
  • Escherichia coli Proteins
  • AmpC beta-lactamases
  • beta-Lactamases