ArticleThe Journal of biological chemistry2011
Studies of the mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.
- Past, Present and Future of Chemodenervation with Botulinum Toxin in the Treatment of Overactive Bladder.The Journal of urology · 2017Pooled it
- The Role of a Conserved Arg-Asp Pair in the Structure and Function of Tetanus Neurotoxin.Toxins · 2025Article
- In Silico Conformational Features of Botulinum Toxins A1 and E1 According to Intraluminal Acidification.Toxins · 2022Article
- Spectroscopic evidence of tetanus toxin translocation domain bilayer-induced refolding and insertion.Biophysical journal · 2021Article
- Sleep/wake calcium dynamics, respiratory function, and ROS production in cardiac mitochondria.Journal of advanced research · 2021Article
- Structural flexibility of the tetanus neurotoxin revealed by crystallographic and solution scattering analyses.Journal of structural biology: X · 2021Article
- Pharmacological Management of Urinary Incontinence: Current and Emerging Treatment.Clinical pharmacology : advances and applications · 2021Review
- Two VHH Antibodies Neutralize Botulinum Neurotoxin E1 by Blocking Its Membrane Translocation in Host Cells.Toxins · 2020Article
- Resolving the Molecular Steps in Clostridial Neurotoxin Light Chain Translocation.Journal of experimental neurology · 2020Article
- A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1.Nature communications · 2018Article
- Structural and functional analysis of botulinum neurotoxin subunits for pH-dependent membrane channel formation and translocation.Biochimica et biophysica acta · 2015Article
- Review
- Beltless translocation domain of botulinum neurotoxin A embodies a minimum ion-conductive channel.The Journal of biological chemistry · 2012Article
- Structures of engineered Clostridium botulinum neurotoxin derivatives.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Botulinum neurotoxin (BoNT) belongs to a large class of toxic proteins that act by enzymatically modifying cytosolic substrates within eukaryotic cells. The process by which a catalytic moiety is transferred across a membrane to enter the cytosol is not understood for any such toxin. BoNT is known to form pH-dependent pores important for the translocation of the catalytic domain into the cytosol. As a first step toward understanding this process, we investigated the mechanism by which the translocation domain of BoNT associates with a model liposome membrane. We report conditions that allow pH-dependent proteoliposome formation and identify a sequence at the translocation domain C terminus that is protected from proteolytic degradation in the context of the proteoliposome. Fluorescence quenching experiments suggest that residues within this sequence move to a hydrophobic environment upon association with liposomes. EPR analyses of spin-labeled mutants reveal major conformational changes in a distinct region of the structure upon association and indicate the formation of an oligomeric membrane-associated intermediate. Together, these data support a model of how BoNT orients with membranes in response to low pH.
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Registered trials
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