| Literature DB >> 26823169 |
Manuella Catel-Ferreira1, Sara Marti1,2, Laurent Guillon3, Luis Jara4, Gaël Coadou5, Virginie Molle6, Emeline Bouffartigues7, German Bou8, Isabelle Shalk3, Thierry Jouenne1, Xavier Vila-Farrés2, Emmanuelle Dé1.
Abstract
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 ΔompW 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.Entities:
Keywords: colistin resistance; hydrophobic channel; iron homeostasis
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Year: 2016 PMID: 26823169 DOI: 10.1002/1873-3468.12050
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124