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. 2012 Nov 7;4(11):1196–1222. doi: 10.3390/toxins4111196

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© 2012 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

PMC Copyright notice

Botulinum neurotoxin blocking Ach release from the neuromuscular junction. The heavy chain (Hc) of neurotoxin binds to the presynaptic array of receptors exposed during vesicle recycling. The carboxyl terminal of Hc binds to specific gangliosides and proteins associated with the vesicle membrane (Syt and SV2 isoforms). Lateral movements of the exposed membrane increase the contact of BoNT with more proteins of the presynaptic receptor complex, and the molecule is endocytosed. The intravesicle acidification dissociates the Lc from Hc, and then the amino region of the heavy chain participates in the translocation of Lc into the cytoplasm to cleave specific proteins from the SNAREv and SNAREt complex according the neurotoxin subtype. BoNT/A, C, E target SNAP-25, BoNT/C also cleave syntaxin and BoNT/B, D, F, G target VAMP. The final result is blocking of the Ach release, preventing postsynaptic receptors activation.