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

Thoma, Johannes; Manioglu, Selen; Kalbermatter, David; Bosshart, Patrick; Fotiadis, Dimitrios José; Müller, Daniel J (2018). Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies. Communications biology, 1(23), p. 23. Springer Nature 10.1038/s42003-018-0027-5

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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 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.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Kalbermatter, David; Bosshart, Patrick and Fotiadis, Dimitrios José

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health

ISSN:

2399-3642

Publisher:

Springer Nature

Language:

English

Submitter:

Barbara Järmann-Bangerter

Date Deposited:

27 Feb 2019 10:54

Last Modified:

03 Mar 2019 02:36

Publisher DOI:

10.1038/s42003-018-0027-5

PubMed ID:

30271910

BORIS DOI:

10.7892/boris.124485

URI:

https://boris.unibe.ch/id/eprint/124485

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