High-resolution crystal structures of the botulinum neurotoxin binding domains from subtypes A5 and A6

Jonathan R. Davies, Amy Britton, Sai Man Liu, K. Ravi Acharya

Research output: Contribution to journalArticlepeer-review

Abstract

Clostridium botulinum neurotoxins (BoNTs) cause flaccid paralysis through inhibition of acetylcholine release from motor neurons; however, at tiny doses, this property is exploited for use as a therapeutic. Each member of the BoNT family of proteins consists of three distinct domains: a binding domain that targets neuronal cell membranes (HC), a translocation domain (HN) and a catalytic domain (LC). Here, we present high-resolution crystal structures of the binding domains of BoNT subtypes/A5 (HC/A5) and/A6 (HC/A6). These structures show that the core fold identified in other subtypes is maintained, but with subtle differences at the expected receptor-binding sites.

Original languageEnglish
Pages (from-to)1474-1481
Number of pages8
JournalFEBS Open Bio
Volume10
Issue number8
Early online date23 Jul 2020
DOIs
Publication statusPublished - 1 Aug 2020

Keywords

  • binding domain structure
  • botulinum neurotoxin
  • Clostridium botulinum
  • subtypes
  • X-ray crystallography

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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