Membrane localization and topology of the DnpA protein control fluoroquinolone tolerance in Pseudomonas aeruginosa

FEMS Microbiol Lett. 2016 Sep;363(17):fnw184. doi: 10.1093/femsle/fnw184. Epub 2016 Jul 31.

Abstract

DnpA, a putative de-N-acetylase of the PIG-L superfamily, is required for antibiotic tolerance in Pseudomonas aeruginosa Exactly how dnpA (gene locus PA5002) directs the formation of antibiotic-tolerant persister cells is currently unknown. Previous research provided evidence for a role in surface-associated process(es), possibly in lipopolysaccharide biosynthesis. In silico sequence analysis of DnpA predicts a single transmembrane domain and Nin/Cout orientation of DnpA. In contrast, we here show that DnpA is an integral inner membrane protein containing two transmembrane domains, with the major C-terminal part located at the cytoplasmic face. Correct insertion into the inner membrane is necessary for DnpA to promote fluoroquinolone tolerance. The membrane localization of DnpA further supports its role in cell envelope-associated process(es). In addition to shedding light on the biological role of DnpA, this study highlights the risks of overreliance on the predictive value of bioinformatics tools and the importance of rigorous experimental validation of in silico predictions.

Keywords: LPS; antibiotic tolerance; cytoplasmic membrane; de-N-acetylase; persistence.

MeSH terms

  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Computer Simulation
  • Fluoroquinolones / metabolism
  • Fluoroquinolones / pharmacology*
  • Lipopolysaccharides / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Pseudomonas aeruginosa / drug effects
  • Pseudomonas aeruginosa / enzymology
  • Pseudomonas aeruginosa / genetics
  • Pseudomonas aeruginosa / metabolism*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Fluoroquinolones
  • Lipopolysaccharides
  • Membrane Proteins