ArticleEMBO reports2022
Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin.
Article in EMBO reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Identification and structural characterization of anthrax toxin receptor 2 as the Clostridium perfringens NetF receptor.Nature communications · 2026Article
- Milestones in Clostridium perfringens research since 1995.Anaerobe · 2025Review
- Review
- Review
- Overview of Bacterial Protein Toxins from Pathogenic Bacteria: Mode of Action and Insights into Evolution.Toxins · 2024Review
- Article
- Bacterial pathogens deliver water/solute-permeable channels as a virulence strategy.bioRxiv : the preprint server for biology · 2023Article
- Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin.EMBO reports · 2022Article
- Detergent Alternatives: Membrane Protein Purification Using Synthetic Nanodisc Polymers.Methods in molecular biology (Clifton, N.J.) · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clostridium perfringens is one of the most widely distributed and successful pathogens producing an impressive arsenal of toxins. One of the most potent toxins produced is the C. perfringens β-toxin (CPB). This toxin is the main virulence factor of type C strains. We describe the cryo-electron microscopy (EM) structure of CPB oligomer. We show that CPB forms homo-octameric pores like the hetero-oligomeric pores of the bi-component leukocidins, with important differences in the receptor binding region and the N-terminal latch domain. Intriguingly, the octameric CPB pore complex contains a second 16-stranded β-barrel protrusion atop of the cap domain that is formed by the N-termini of the eight protomers. We propose that CPB, together with the newly identified Epx toxins, is a member a new subclass of the hemolysin-like family. In addition, we show that the β-barrel protrusion domain can be modified without affecting the pore-forming ability, thus making the pore particularly attractive for macromolecule sensing and nanotechnology. The cryo-EM structure of the octameric pore of CPB will facilitate future developments in both nanotechnology and basic research.
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