ArticleCell host & microbe2011
Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly.
Article in Cell host & microbe, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 64 citations in OpenAlex.
- Structure of the complete 14-subunit botulinum neurotoxin B complex reveals a unique anchoring through the narrow central pore of HA70.Science advances · 2025Article
- A Comprehensive Structural Analysis ofToxins · 2023Review
- In Silico Conformational Features of Botulinum Toxins A1 and E1 According to Intraluminal Acidification.Toxins · 2022Article
- Molecular landscape of BoNT/B bound to a membrane-inserted synaptotagmin/ganglioside complex.Cellular and molecular life sciences : CMLS · 2022Article
- Detection of VAMP Proteolysis by Tetanus and Botulinum Neurotoxin Type B In Vivo with a Cleavage-Specific Antibody.International journal of molecular sciences · 2022Article
- Exceptionally potent human monoclonal antibodies are effective for prophylaxis and treatment of tetanus in mice.The Journal of clinical investigation · 2021Article
- Spectroscopic evidence of tetanus toxin translocation domain bilayer-induced refolding and insertion.Biophysical journal · 2021Article
- Use of Crystallography and Molecular Modeling for the Inhibition of the Botulinum Neurotoxin A Protease.ACS medicinal chemistry letters · 2021Article
- Irreversible inhibition of BoNT/A protease: proximity-driven reactivity contingent upon a bifunctional approach.RSC medicinal chemistry · 2021Article
- Structural Insights into Rational Design of Single-Domain Antibody-Based Antitoxins against Botulinum Neurotoxins.Cell reports · 2020Article
- 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
- A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1.Nature communications · 2018Article
- Review
- Review
- A lipid-binding loop of botulinum neurotoxin serotypes B, DC and G is an essential feature to confer their exquisite potency.PLoS pathogens · 2018Article
- Review
- Cysteine residues in a yeast viral A/B toxin crucially control host cell killing via pH-triggered disulfide rearrangements.Molecular biology of the cell · 2017Article
- Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology.Pharmacological reviews · 2017Review
- Neuronal entry and high neurotoxicity of botulinum neurotoxin A require its N-terminal binding sub-domain.Scientific reports · 2017Article
- Article
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7 authors at 3 institutions in 2 countries.
Funding
Abstract
Botulinum neurotoxins (BoNTs, serotypes A-G), elaborated by Clostridium botulinum, can induce lethal paralysis and are classified as Category A bioterrorism agents. However, how BoNTs translocate from endosomes into the cytosol of neurons to gain access to their intracellular targets remains enigmatic. We discovered that binding to the ganglioside GT1b, a toxin coreceptor, enables BoNT/B to sense low pH, undergo a significant change in secondary structure, and transform into a hydrophobic oligomeric membrane protein. Imaging of the toxin on lipid bilayers using atomic force microscopy revealed donut-shaped channel-like structures that resemble other protein translocation assemblies. Toosendanin, a drug with therapeutic effects against botulism, inhibited GT1b-dependent BoNT/B oligomerization and in parallel truncated BoNT/B single-channel conductance, suggesting that oligomerization plays a role in the translocation reaction. Thus, BoNT/B functions as a coincidence detector for receptor and low pH to ensure spatial and temporal accuracy for toxin conversion into a translocation channel.
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Registered trials
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.