4.3 Article

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

Journal

FEMS MICROBIOLOGY LETTERS
Volume 296, Issue 2, Pages 241-247

Publisher

OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2009.01651.x

Keywords

Pseudomonas aeruginosa; outer membrane; OprG; anaerobic; porin

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Funding

  1. Canadian Cystic Fibrosis Foundation
  2. Canadian Institutes of Health Research
  3. CCFF

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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.

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