Open AccessThe major outer membrane protein OprG of Pseudomonas aeruginosa contributes to cytotoxicity and forms an anaerobically regulated, cation‐selective channel
Author(s) -
McPhee Joseph B.,
Tamber Sandeep,
Bains Manjeet,
Maier Elke,
Gellatly Shaan,
Lo Andy,
Benz Roland,
Hancock Robert E.W.
Publication year - 2009
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2009.01651.x
Subject(s) - pseudomonas aeruginosa , bacterial outer membrane , chemistry , cytotoxic t cell , regulator , microbiology and biotechnology , cytotoxicity , bacteria , membrane , biophysics , membrane protein , biology , biochemistry , escherichia coli , in vitro , gene , genetics
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.