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TitleCryo-EM structure of the octameric pore of Clostridium perfringens β-toxin.
Journal, issue, pagesEMBO Rep, Vol. 23, Issue 12, Page e54856, Year 2022
Publish dateDec 6, 2022
AuthorsJulia Bruggisser / Ioan Iacovache / Samuel C Musson / Matteo T Degiacomi / Horst Posthaus / Benoît Zuber /
PubMed AbstractClostridium 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 ...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.
External linksEMBO Rep / PubMed:36215680 / PubMed Central
MethodsEM (single particle)
Resolution3.84 Å
Structure data

13876

7q9y

EMDB-13876, PDB-7q9y:
Cryo-EM structure of the octameric pore of Clostridium perfringens beta-toxin.
Method: EM (single particle) / Resolution: 3.84 Å

Source
  • Clostridium perfringens (bacteria)
  • clostridium perfringens cpe (bacteria)
KeywordsTOXIN / pore forming toxin / hemolysin / octamer

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