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

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 characterist...

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Autores principales: Thoma, Johannes, Manioglu, Selen, Kalbermatter, David, Bosshart, Patrick D., Fotiadis, Dimitrios, Müller, Daniel J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6123736/
https://www.ncbi.nlm.nih.gov/pubmed/30271910
http://dx.doi.org/10.1038/s42003-018-0027-5
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author Thoma, Johannes
Manioglu, Selen
Kalbermatter, David
Bosshart, Patrick D.
Fotiadis, Dimitrios
Müller, Daniel J.
author_facet Thoma, Johannes
Manioglu, Selen
Kalbermatter, David
Bosshart, Patrick D.
Fotiadis, Dimitrios
Müller, Daniel J.
author_sort Thoma, Johannes
collection PubMed
description 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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spelling pubmed-61237362018-09-28 Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies Thoma, Johannes Manioglu, Selen Kalbermatter, David Bosshart, Patrick D. Fotiadis, Dimitrios Müller, Daniel J. Commun Biol Article 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. Nature Publishing Group UK 2018-04-05 /pmc/articles/PMC6123736/ /pubmed/30271910 http://dx.doi.org/10.1038/s42003-018-0027-5 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Thoma, Johannes
Manioglu, Selen
Kalbermatter, David
Bosshart, Patrick D.
Fotiadis, Dimitrios
Müller, Daniel J.
Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies
title Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies
title_full Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies
title_fullStr Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies
title_full_unstemmed Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies
title_short Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies
title_sort protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6123736/
https://www.ncbi.nlm.nih.gov/pubmed/30271910
http://dx.doi.org/10.1038/s42003-018-0027-5
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