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  HIV-1 gp41 transmembrane oligomerization monitored by FRET and FCS.

Schroeder, S., Kaufmann, J. D., Grunwald, M., Walla, P. J., Lakomek, N. A., & Wingfield, P. T. (2018). HIV-1 gp41 transmembrane oligomerization monitored by FRET and FCS. FEBS Letters, 592(6), 939-948. doi:10.1002/1873-3468.13010.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-8149-C Version Permalink: http://hdl.handle.net/21.11116/0000-0000-FF8F-1
Genre: Journal Article

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 Creators:
Schroeder, S., Author
Kaufmann, J. D., Author
Grunwald, M., Author
Walla, P. J.1, Author              
Lakomek, N. A.2, Author              
Wingfield, P. T., Author
Affiliations:
1Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society, ou_578565              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: HIV ; fluorescence spectroscopy; gp41; membrane fusion; monomer-trimer equilibrium; structural biology
 Abstract: The HIV-1 envelope gp120/gp41 trimer mediates viral membrane fusion. After CD-4 recognition, gp120 detaches from the virus, exposing gp41 which triggers fusion. During the fusion process, gp41 may not remain trimeric, which could have functional importance. Here, we probe the reversible association of full length gp41 (minus the cytoplasmic domain) in detergent micelles (with probes attached to transmembrane domain) by fluorescence resonance energy transfer (FRET) with a μM dissociation constant. This is compared with other methods. A gp41-targeted fusion inhibitor must interfere with this transition, and monomeric, partially monomeric or trimeric states all present potential binding epitopes. The gp41 self-association is a valid drug target model and FRET, a potential high-throughput assay system, could be used to screen drug libraries. This article is protected by copyright. All rights reserved.

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Language(s): eng - English
 Dates: 2018-02-172018-03
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/1873-3468.13010
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 592 (6) Sequence Number: - Start / End Page: 939 - 948 Identifier: -