ArticlePLoS pathogens2018
A lipid-binding loop of botulinum neurotoxin serotypes B, DC and G is an essential feature to confer their exquisite potency.
Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Advances in Clostridial Neurotoxins: Passage of the Intestinal Barrier and Targeting of Specific Neuronal Cells.Toxins · 2026Review
- Botulinum Toxin Therapy: A Comprehensive Review on Clinical and Pharmacological Insights.Journal of clinical medicine · 2025Review
- Cryo-EM structure of the botulinum neurotoxin A/SV2B complex and its implications for translocation.Nature communications · 2025Article
- Activity of botulinum neurotoxin X and its structure when shielded by a non-toxic non-hemagglutinin protein.Communications chemistry · 2024Article
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- Article
- The Epigenetic Dimension of Protein Structure Is an Intrinsic Weakness of the AlphaFold Program.Biomolecules · 2022Article
- Molecular landscape of BoNT/B bound to a membrane-inserted synaptotagmin/ganglioside complex.Cellular and molecular life sciences : CMLS · 2022Article
- Innovative and Highly Sensitive Detection ofToxins · 2021Article
- New approach for the rational selection of markers to identify botulinum toxins.Archives of toxicology · 2021Article
- Botulinum Neurotoxins: Mechanism of Action.Handbook of experimental pharmacology · 2021Review
- Characterization of a membrane binding loop leads to engineering botulinum neurotoxin B with improved therapeutic efficacy.PLoS biology · 2020Article
- Structural Insights into Rational Design of Single-Domain Antibody-Based Antitoxins against Botulinum Neurotoxins.Cell reports · 2020Article
- Neurons, Glia, Extracellular Matrix and Neurovascular Unit: A Systems Biology Approach to the Complexity of Synaptic Plasticity in Health and Disease.International journal of molecular sciences · 2020Review
- Gangliosides interact with synaptotagmin to form the high-affinity receptor complex for botulinum neurotoxin B.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Sensitive detection of type G botulinum neurotoxin through Endopep-MS peptide substrate optimization.Analytical and bioanalytical chemistry · 2019Article
- A neurotoxin that specifically targets Anopheles mosquitoes.Nature communications · 2019Article
- Botulinum and Tetanus Neurotoxins.Annual review of biochemistry · 2019Review
- Functional detection of botulinum neurotoxin serotypes A to F by monoclonal neoepitope-specific antibodies and suspension array technology.Scientific reports · 2019Article
- The analgesic effect of intraarticular OnabotulinumtoxinA in a female murine model of collagenase induced chronic degenerative monoarthritis.Toxicon : official journal of the International Society on Toxinology · 2019Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The exceptional toxicity of botulinum neurotoxins (BoNTs) is mediated by high avidity binding to complex polysialogangliosides and intraluminal segments of synaptic vesicle proteins embedded in the presynaptic membrane. One peculiarity is an exposed hydrophobic loop in the toxin's cell binding domain HC, which is located between the ganglioside- and protein receptor-binding sites, and that is particularly pronounced in the serotypes BoNT/B, DC, and G sharing synaptotagmin as protein receptor. Here, we provide evidence that this HC loop is a critical component of their tripartite receptor recognition complex. Binding to nanodisc-embedded receptors and toxicity were virtually abolished in BoNT mutants lacking residues at the tip of the HC loop. Surface plasmon resonance experiments revealed that only insertion of the HC loop into the lipid-bilayer compensates for the entropic penalty inflicted by the dual-receptor binding. Our results represent a new paradigm of how BoNT/B, DC, and G employ ternary interactions with a protein, ganglioside, and lipids to mediate their extraordinary neurotoxicity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.