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Botulinum neurotoxin A1 likes it double sweet

Nature Structural & Molecular Biology volume 23, pages 619–621 (2016)Cite this article

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The pathogenesis of the nerve paralysis induced by botulinum neurotoxins begins with their specific and high-affinity binding to peripheral nerve terminals. The new crystal structure of the toxin bound to its glycosylated receptor, presented in this issue, represents a major step forward in the understanding of how botulinum neurotoxin type A1, the toxin used in human therapy and cosmetics, binds its protein receptor.

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Figure 1: Molecular interactions of the N-linked glycan moiety of SV2C to BoNT/A1.
Figure 2: Cartoon representation of the complex of BoNT/A1 with glycosylated SVC2 (left, PDB 5JLV7,ganglioside modeled in) and BoNT/B1 with synaptotagmin and ganglioside (right, PDB 4KBB19).

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Authors and Affiliations

  1. Cesare Montecucco and Giuseppe Zanotti are at the Department of Biomedical Sciences, University of Padova, Padova, Italy.,

    Cesare Montecucco & Giuseppe Zanotti

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  1. Cesare Montecucco
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  2. Giuseppe Zanotti
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Correspondence to Cesare Montecucco or Giuseppe Zanotti.

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Montecucco, C., Zanotti, G. Botulinum neurotoxin A1 likes it double sweet. Nat Struct Mol Biol 23, 619–621 (2016). https://doi.org/10.1038/nsmb.3253

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