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Updated: Feb 12, 2026

A High Content Imaging Assay for Identification of Botulinum Neurotoxin Inhibitors
Published on: November 14, 2014
High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and
Jonathan R Davies1, Gavin S Hackett2, Sai Man Liu2
1Department of Biology and Biochemistry, University of Bath, Bath, United Kingdom.
Abstract:
The binding specificity of botulinum neurotoxins (BoNTs) is primarily a consequence of their ability to bind to multiple receptors at the same time. BoNTs consist of three distinct domains, a metalloprotease light chain (LC), a translocation domain (HN) and a receptor-binding domain (HC). Here we report the crystal structure of HC/FA, complementing an existing structure through the modelling of a previously unresolved loop which is important for receptor-binding. Our HC/FA structure also contains a previously unidentified disulphide bond, which we have also observed in one of two crystal forms of HC/A1. This may have implications for receptor-binding and future recombinant toxin production.
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