7Q9Y

Cryo-EM structure of the octameric pore of Clostridium perfringens beta-toxin.

(2022) EMBO Rep 23: e54856-e54856

• PubMed: 36215680 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.15252/embr.202254856
• Primary Citation of Related Structures:  
  7Q9Y


• PubMed 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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Organizational Affiliation: 

Institute of Animal Pathology, Vetsuisse-Faculty, University of Bern, Bern, Switzerland.