High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA

Jonathan R Davies, Gavin S Hackett, Sai Man Liu, K Ravi Acharya

Research output: Contribution to journalArticle

3 Citations (Scopus)

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.

Original languageEnglish
Article numbere4552
JournalPeerJ
Volume6
DOIs
Publication statusPublished - 21 Mar 2018

Keywords

  • Botulinum neurotoxin
  • Crystal structure
  • FA hybrid
  • Receptor binding domain
  • SV2
  • Targeted secretion inhibitor

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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