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High resolution crystal structures of Clostridium botulinum neurotoxin A3 and A4 binding domains

DOI: 10.1016/j.jsb.2017.12.010 DOI Help

Authors: Jonathan R. Davies (University of Bath) , Jay Rees (University of Bath) , Sai Man Liu (Ipsen Bioinnovation Limited) , K. Ravi Acharya (University of Bath)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Journal Of Structural Biology

State: Published (Approved)
Published: December 2017
Diamond Proposal Number(s): 12342

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.

Journal Keywords: Clostridium botulinum; Botulinum neurotoxin; Subtypes; Binding domain structure; Crystallography

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I03-Macromolecular Crystallography

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