The crystal structure of Bacillus cereus HblL1

DOI: 10.3390/toxins13040253

Authors: Harley L. Worthy (Cardiff University; Exeter University) , Lainey J. Williamson (Cardiff University) , Husam Sabah Auhim (Cardiff University; University of Baghdad) , Stephen H. Leppla (National Institute of Allergy and Infectious Diseases, National Institutes of Health) , Inka Sastalla (National Institute of Allergy and Infectious Diseases, National Institutes of Health) , D. Dafydd Jones (Cardiff University) , Pierre J. Rizkallah (Cardiff University) , Colin Berry (Cardiff University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Toxins , VOL 13

State: Published (Approved)
Published: March 2021
Diamond Proposal Number(s): 18812

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.

Journal Keywords: tripartite toxin; hemolytic toxin; haemolytic toxin; Bacillus cereus

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials


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

Discipline Tags:

Life Sciences & Biotech Health & Wellbeing Pathogens Structural biology

Technical Tags:

Diffraction Macromolecular Crystallography (MX)