The major outer membrane protein OprG of Pseudomonas aeruginosa contributes to cytotoxicity and forms an anaerobically regulated, cation-selective channel

FEMS Microbiol Lett. 2009 Jun;296(2):241-7. doi: 10.1111/j.1574-6968.2009.01651.x. Epub 2009 May 14.


OprG of Pseudomonas aeruginosa is a member of the very large and widely distributed but poorly characterized OmpW (PF0392) family of outer membrane proteins. It was established here that OprG was highly transcribed in anaerobic environments rich in iron via the ANR regulator. In the absence of OprG, P. aeruginosa was significantly less cytotoxic toward human bronchial epithelial cells. Planar bilayer studies indicated that purified OprG formed cationic-selective channels with a conductance of 500 pS in 1 M KCl; however, contrary to previous reports, OprG did not appear to be involved in either iron or antibiotic uptake.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anaerobiosis
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Outer Membrane Proteins / toxicity*
  • Cations / metabolism*
  • Cell Line
  • Epithelial Cells / microbiology
  • Gene Expression Profiling
  • Humans
  • Ion Channels / metabolism*
  • Ion Channels / toxicity*
  • Iron / metabolism
  • Pseudomonas aeruginosa / metabolism*
  • Pseudomonas aeruginosa / pathogenicity*
  • Respiratory Mucosa / microbiology


  • Bacterial Outer Membrane Proteins
  • Cations
  • Ion Channels
  • OprG protein, Pseudomonas aeruginosa
  • Iron