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The outer membrane porin OmpW of Acinetobacter baumannii is involved in iron uptake and colistin binding
Author(s) -
CatelFerreira Manuella,
Marti Sara,
Guillon Laurent,
Jara Luis,
Coadou Gaël,
Molle Virginie,
Bouffartigues Emeline,
Bou German,
Shalk Isabelle,
Jouenne Thierry,
VilaFarrés Xavier,
Dé Emmanuelle
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12050
Subject(s) - porin , acinetobacter baumannii , bacterial outer membrane , colistin , imipenem , microbiology and biotechnology , chemistry , mutant , biology , biochemistry , bacteria , antibiotic resistance , antibiotics , genetics , gene , escherichia coli , pseudomonas aeruginosa
This study was undertaken to characterize functions of the outer membrane protein OmpW, which potentially contributes to the development of colistin‐ and imipenem‐resistance in Acinetobacter baumannii . Reconstitution of OmpW in artificial lipid bilayers showed that it forms small channels (23 pS in 1 m KCl) and markedly interacts with iron and colistin, but not with imipenem. In vivo, 55 Fe uptake assays comparing the behaviours of Δ ompW mutant and wild‐type strains confirmed a role for OmpW in A. baumannii iron homeostasis. However, the loss of OmpW expression did not have an impact on A. baumannii susceptibilities to colistin or imipenem.