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HIV ‐1 gp41 transmembrane oligomerization monitored by FRET and FCS
Author(s) -
Schroeder Sabrina,
Kaufman Joshua D.,
Grunwald Matthias,
Walla Peter J.,
Lakomek NilsAlexander,
Wingfield Paul T.
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13010
Subject(s) - gp41 , förster resonance energy transfer , chemistry , trimer , lipid bilayer fusion , biophysics , transmembrane protein , fusion , piezo1 , dissociation constant , biochemistry , epitope , microbiology and biotechnology , fluorescence , membrane , ion channel , biology , antibody , dimer , receptor , physics , linguistics , organic chemistry , philosophy , quantum mechanics , immunology , mechanosensitive channels
The HIV ‐1 envelope gp120/gp41 trimer mediates viral membrane fusion. After cluster of differentiation‐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 μ m 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.