Membrane Fusion Mediated by Non-covalent Binding of Re-engineered Cholera Toxin Assemblies to Glycolipids.

Autor:	Wehrum S; Faculty of Biology, Albert-Ludwigs-University Freiburg, Schänzlestraße 1, 79104 Freiburg, Germany.; Bioss-Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, Schänzlestraße 18, 79104 Freiburg, Germany., Siukstaite L; Faculty of Biology, Albert-Ludwigs-University Freiburg, Schänzlestraße 1, 79104 Freiburg, Germany.; Bioss-Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, Schänzlestraße 18, 79104 Freiburg, Germany., Williamson DJ; School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, U.K.., Branson TR; School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, U.K.., Sych T; Faculty of Biology, Albert-Ludwigs-University Freiburg, Schänzlestraße 1, 79104 Freiburg, Germany.; Bioss-Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, Schänzlestraße 18, 79104 Freiburg, Germany.; Freiburg Center for Interactive Materials and Bioinspired Technology (FIT), Albert-Ludwigs-University Freiburg, Georges-Köhler-Allee 105, 79110 Freiburg, Germany.; Science for Life Laboratory, Department of Women's and Children's Health, Karolinska Institutet, 17165 Solna, Sweden., Madl J; Faculty of Biology, Albert-Ludwigs-University Freiburg, Schänzlestraße 1, 79104 Freiburg, Germany.; Bioss-Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, Schänzlestraße 18, 79104 Freiburg, Germany.; Freiburg Center for Interactive Materials and Bioinspired Technology (FIT), Albert-Ludwigs-University Freiburg, Georges-Köhler-Allee 105, 79110 Freiburg, Germany., Wildsmith GC; School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, U.K.., Dai W; School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, U.K.., Kempmann E; Faculty of Biology, Albert-Ludwigs-University Freiburg, Schänzlestraße 1, 79104 Freiburg, Germany.; Bioss-Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, Schänzlestraße 18, 79104 Freiburg, Germany., Ross JF; School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, U.K.., Thomsen M; School of Biomedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, U.K.., Webb ME; School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, U.K.., Römer W; Faculty of Biology, Albert-Ludwigs-University Freiburg, Schänzlestraße 1, 79104 Freiburg, Germany.; Bioss-Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, Schänzlestraße 18, 79104 Freiburg, Germany.; Freiburg Center for Interactive Materials and Bioinspired Technology (FIT), Albert-Ludwigs-University Freiburg, Georges-Köhler-Allee 105, 79110 Freiburg, Germany., Turnbull WB; School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT Leeds, U.K..
Jazyk:	angličtina
Zdroj:	ACS synthetic biology [ACS Synth Biol] 2022 Dec 16; Vol. 11 (12), pp. 3929-3938. Date of Electronic Publication: 2022 Nov 11.
DOI:	10.1021/acssynbio.2c00266
Abstrakt:	Membrane fusion is essential for the transport of macromolecules and viruses across membranes. While glycan-binding proteins (lectins) often initiate cellular adhesion, subsequent fusion events require additional protein machinery. No mechanism for membrane fusion arising from simply a protein binding to membrane glycolipids has been described thus far. Herein, we report that a biotinylated protein derived from cholera toxin becomes a fusogenic lectin upon cross-linking with streptavidin. This novel reengineered protein brings about hemifusion and fusion of vesicles as demonstrated by mixing of fluorescently labeled lipids between vesicles as well as content mixing of liposomes filled with fluorescently labeled dextran. Exclusion of the complex at vesicle-vesicle interfaces could also be observed, indicating the formation of hemifusion diaphragms. Discovery of this fusogenic lectin complex demonstrates that new emergent properties can arise from simple changes in protein architecture and provides insights into new mechanisms of lipid-driven fusion.
Databáze:	MEDLINE
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