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

DOI: 10.7717/peerj.4552 DOI Help

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

Type: Journal Paper
Journal: Peerj , VOL 6

State: Published (Approved)
Published: March 2018
Diamond Proposal Number(s): 8922 , 12342

Open Access Open Access

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.

Journal Keywords: SV2; Crystal structure; Botulinum neurotoxin; Targeted secretion inhibitor; FA hybrid; Receptor binding domain

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

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