Effect of membrane fusion protein AdeT1 on the antimicrobial resistance of Escherichia coli

Sci Rep. 2020 Nov 24;10(1):20464. doi: 10.1038/s41598-020-77339-w.

Abstract

Acinetobacter baumannii is a prevalent pathogen that can rapidly acquire resistance to antibiotics. Indeed, multidrug-resistant A. baumannii is a major cause of hospital-acquired infections and has been recognised by the World Health Organization as one of the most threatening bacteria to our society. Resistance-nodulation-division (RND) type multidrug efflux pumps have been demonstrated to convey antibiotic resistance to a wide range of pathogens and are the primary resistance mechanism employed by A. baumannii. A component of an RND pump in A. baumannii, AdeT1, was previously demonstrated to enhance the antimicrobial resistance of Escherichia coli. Here, we report the results of experiments which demonstrate that wild-type AdeT1 does not confer antimicrobial resistance in E. coli, highlighting the importance of verifying protein production when determining minimum inhibitory concentrations (MICs) especially by broth dilution. Nevertheless, using an agar-based MIC assay, we found that propionylation of Lys280 on AdeT1 renders E. coli cells more resistant to erythromycin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acinetobacter baumannii / drug effects
  • Acinetobacter baumannii / genetics
  • Acinetobacter baumannii / growth & development*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Drug Resistance, Multiple, Bacterial
  • Erythromycin / pharmacology*
  • Escherichia coli / drug effects
  • Escherichia coli / genetics
  • Escherichia coli / growth & development*
  • Lysine / metabolism
  • Membrane Fusion
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Microbial Sensitivity Tests
  • Recombinant Proteins / metabolism

Substances

  • Bacterial Proteins
  • Membrane Proteins
  • Recombinant Proteins
  • Erythromycin
  • Lysine