Gangliosides interact with synaptotagmin to form the high-affinity receptor complex for botulinum neurotoxin B

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 116; no. 36; pp. 18098 - 18108
• Main Authors: Flores, Alessandra, Ramirez-Franco, Jorge, Desplantes, Richard, Debreux, Kévin, Ferracci, Géraldine, Wernert, Florian, Blanchard, Marie-Pierre, Maulet, Yves, Youssouf, Fahamoe, Sangiardi, Marion, Iborra, Cécile, Popoff, Michel Robert, Seagar, Michael, Fantini, Jacques, Lévêque, Christian, Far, Oussama El
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 03.09.2019
• Series: PNAS Plus
• Subjects: Affinity; Animals; Binding; Binding Sites; Biological Sciences; Botulinum toxin; Botulinum toxin type B; Botulinum Toxins, Type A - chemistry; Botulinum Toxins, Type A - metabolism; Cellular Biology; Ceramide; Circular dichroism; Dichroism; Domains; Fluorescence; Fluorescence spectroscopy; Gangliosides; Gangliosides - chemistry; Gangliosides - pharmacology; Life Sciences; Molecular modelling; Molecular structure; Monomolecular films; Mutation; Nerve endings; Neurotoxins; Oligosaccharides; Peptides; PNAS Plus; Point mutation; Potentiation; Protein Conformation, alpha-Helical; Protein Domains; Rats; Surface plasmon resonance; Synaptotagmin; Synaptotagmin I - chemistry; Synaptotagmin I - genetics; Synaptotagmin I - metabolism; Synaptotagmin II - chemistry; Synaptotagmin II - genetics; Synaptotagmin II - metabolism; Toxins; Transmembrane domains; Tryptophan; gangliosides; synaptotagmin; botulinum neurotoxin B receptor

Botulinum neurotoxin type B (BoNT/B) recognizes nerve terminals by binding to 2 receptor components: a polysialoganglioside, predominantly GT1b, and synaptotagmin 1/2. It is widely thought that BoNT/B initially binds to GT1b then diffuses in the plane of the membrane to interact with synaptotagmin....