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

DOI: 10.1002/2211-5463.12931 DOI Help

Authors: Jonathan R. Davies (University of Bath; Stockholm University) , Amy Britton (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: Febs Open Bio

State: Published (Approved)
Published: July 2020
Diamond Proposal Number(s): 17212

Open Access Open Access

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.

Journal Keywords: Clostridium botulinum; Botulinum neurotoxin; Subtypes; Binding domain structure; X‐ray crystallography

Diamond Keywords: Botulism; Bacteria

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 22/07/2020 10:45

Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)