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Updated: Feb 16, 2026
A High Content Imaging Assay for Identification of Botulinum Neurotoxin Inhibitors
Published on: November 14, 2014
High resolution crystal structures of Clostridium botulinum neurotoxin A3 and A4 binding domains
Jonathan R Davies1, Jay Rees1, Sai Man Liu2
1Department of Biology and Biochemistry, Claverton Down, University of Bath, Bath BA2 7AY, UK.
Abstract:
Clostridium botulinum neurotoxins (BoNTs) cause the life-threatening condition, botulism. However, while they have the potential to cause serious harm, they are increasingly being utilised for therapeutic applications. BoNTs comprise of seven distinct serotypes termed BoNT/A through BoNT/G, with the most widely characterised being sub-serotype BoNT/A1. Each BoNT consists of three structurally distinct domains, a binding domain (HC), a translocation domain (HN), and a proteolytic domain (LC). The HC domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. Here, we present two high-resolution structures of the binding domain of subtype BoNT/A3 (HC/A3) and BoNT/A4 (HC/A4) at 1.6 Å and 1.34 Å resolution, respectively. The structures of both proteins share a high degree of similarity to other known BoNT HC domains whilst containing some subtle differences, and are of benefit to research into therapeutic neurotoxins with novel characteristics.
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