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Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Thoma Johannes, Manioglu Selen, Kalbermatter David, Bosshart Patrick D., Fotiadis Dimitrios, Müller Daniel J.,
Project Structure and supramolecular organization of membrane transport proteins
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Original article (peer-reviewed)

Journal Communications Biology
Volume (Issue) 1(1)
Page(s) 23 - 23
Title of proceedings Communications Biology
DOI 10.1038/s42003-018-0027-5

Open Access

URL http://doi.org/10.1038/s42003-018-0027-5
Type of Open Access Publisher (Gold Open Access)

Abstract

Most studies characterizing the folding, structure, and function of membrane proteins rely on solubilized or reconstituted samples. Whereas solubilized membrane proteins lack the functionally important lipid membrane, reconstitution embeds them into artificial lipid bilayers, which lack characteristic features of cellular membranes including lipid diversity, composition and asymmetry. Here, we utilize outer membrane vesicles (OMVs) released from Escherichia coli to study outer membrane proteins (Omps) in the native membrane environment. Enriched in the native membrane of the OMV we characterize the assembly, folding, and structure of OmpG, FhuA, Tsx, and BamA. Comparing Omps in OMVs to those reconstituted into artificial lipid membranes, we observe different unfolding pathways for some Omps. This observation highlights the importance of the native membrane environment to maintain the native structure and function relationship of Omps. Our fast and easy approach paves the way for functional and structural studies of Omps in the native membrane.
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