The crystal sructure of Bacillus cereus HblL1

Worthy, Harley L., Williamson, Lainey J., Auhim, Husam Sabah, Leppla, Stephen H., Sastalla, Inka, Jones, D. Dafydd ORCID: https://orcid.org/0000-0001-7709-3995, Rizkallah, Pierre J. ORCID: https://orcid.org/0000-0002-9290-0369 and Berry, Colin ORCID: https://orcid.org/0000-0002-9943-548X 2021. The crystal sructure of Bacillus cereus HblL1. Toxins 13 (4) , 253. 10.3390/toxins13040253

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Abstract

The Hbl toxin is a three-component haemolytic complex produced by Bacillus cereus sensu lato strains and implicated as a cause of diarrhoea in B. cereus food poisoning. While the structure of the HblB component of this toxin is known, the structures of the other components are unresolved. Here, we describe the expression of the recombinant HblL1 component and the elucidation of its structure to 1.36 Å. Like HblB, it is a member of the alpha-helical pore-forming toxin family. In comparison to other members of this group, it has an extended hydrophobic beta tongue region that may be involved in pore formation. Molecular docking was used to predict possible interactions between HblL1 and HblB, and suggests a head to tail dimer might form, burying the HblL1 beta tongue region.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine Biosciences Advanced Research Computing @ Cardiff (ARCCA)
Publisher:	MDPI
ISSN:	2072-6651
Funders:	BBSRC
Date of First Compliant Deposit:	1 April 2021
Date of Acceptance:	29 March 2021
Last Modified:	06 May 2023 09:40
URI:	https://orca.cardiff.ac.uk/id/eprint/140266

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