ArticleStructure (London, England : 1993)2017
Botulinum Toxins A and E Inflict Dynamic Destabilization on t-SNARE to Impair SNARE Assembly and Membrane Fusion.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Combined treatment with antitoxin and 3,4-diaminopyridine improves survival outcomes after lethal botulinum neurotoxin challenge.Molecular medicine (Cambridge, Mass.) · 2025Article
- Review
- A Comparison of Cellular Uptake Mechanisms, Delivery Efficacy, and Intracellular Fate between Liposomes and Extracellular Vesicles.Advanced healthcare materials · 2023Review
- Cancer Drug Delivery Systems Using Bacterial Toxin Translocation Mechanisms.Bioengineering (Basel, Switzerland) · 2023Review
- Functional Deimmunization of Botulinum Neurotoxin Protease Domain via Computationally Driven Library Design and Ultrahigh-Throughput Screening.ACS synthetic biology · 2023Article
- Antidotal treatment of botulism in rats by continuous infusion with 3,4-diaminopyridine.Molecular medicine (Cambridge, Mass.) · 2022Article
- Article
- Proinflammatory macrophage-derived microvesicles exhibit tumor tropism dependent on CCL2/CCR2 signaling axis and promote drug deliveryTheranostics · 2020Article
- EPR Lineshape Analysis to Investigate the SNARE Folding Intermediates.Methods in molecular biology (Clifton, N.J.) · 2019Review
- Alpha-Synuclein Continues to Enhance SNARE-Dependent Vesicle Docking at Exorbitant Concentrations.Frontiers in neuroscience · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Botulinum toxins (BoNTs) A and E block neurotransmitter release by specifically cleaving the C- terminal ends of SNAP-25, a plasma membrane SNARE protein. Here, we find that SNAP-25A and E, the cleavage products of BoNT A and E, respectively, terminate membrane fusion via completely different mechanisms. Combined studies of single-molecule FRET and single-vesicle fusion assays reveal that SNAP-25E is incapable of supporting SNARE pairing and thus, vesicle docking. In contrast, SNAP-25A facilitates robust SNARE pairing and vesicle docking with somewhat reduced SNARE zippering, which leads to severe impairment of fusion pore opening. The electron paramagnetic resonance results show that the discrepancy between SNAP-25A and E might stem from the extent of the dynamic destabilization of the t-SNARE core at the N-terminal half, which plays a pivotal role in nucleating SNARE complex formation. Thus, the results provide insights into the structure/dynamics-based mechanism by which BoNT A and E impair membrane fusion.
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