biostudies-literatureBruggisser JStavros Niarchos FoundationSwiss National Science FoundationEngineering and Physical Sciences Research Councile54856https://www.ebi.ac.uk/biostudies/studies/S-EPMC9724662biostudies-literatureUnknown23(12)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 sEMBO reportsCryo-EM structure of the octameric pore of Clostridium perfringens β-toxin.PMC9724662EP/P016499/116938131003A_16938131003A_179520179520Posthaus HIacovache IZuber BDegiacomi MTBruggisser JMusson SCfalseCryo-EM structure of the octameric pore of Clostridium 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 s2022-01-01T00:00:00Z2022 Dec2026-05-10T06:52:00.627Z2025-02-19T03:26:18.865ZS-EPMC97246623621568010.15252/embr.202254856