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

Joseph B. McPhee, Sandeep Tamber, Manjeet Bains, Elke Maier, Shaan Gellatly, Andy Lo, Roland Benz, Robert E.W. Hancock

Research output: Contribution to journalArticlepeer-review

52 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)241-247
Number of pages7
JournalFEMS Microbiology Letters
Volume296
Issue number2
DOIs
Publication statusPublished or Issued - Jul 2009
Externally publishedYes

Keywords

  • Anaerobic
  • OprG
  • Outer membrane
  • Porin
  • Pseudomonas aeruginosa

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

Cite this