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

Jonathan R. Davies, Jay Rees, Sai Man Liu, K. Ravi Acharya

Research output: Contribution to journalArticlepeer-review

8 Citations (SciVal)

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.

Original languageEnglish
JournalJournal of Structural Biology
Early online date26 Dec 2017
DOIs
Publication statusE-pub ahead of print - 26 Dec 2017

Keywords

  • Binding domain structure
  • Botulinum neurotoxin
  • Clostridium botulinum
  • Crystallography
  • Subtypes

ASJC Scopus subject areas

  • Structural Biology

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