Structural highlights
FunctionPublication Abstract from PubMedClostridium 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 beta-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 beta-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 beta-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. Cryo-EM structure of the octameric pore of Clostridium perfringens beta-toxin.,Bruggisser J, Iacovache I, Musson SC, Degiacomi MT, Posthaus H, Zuber B EMBO Rep. 2022 Dec 6;23(12):e54856. doi: 10.15252/embr.202254856. Epub 2022 Oct , 10. PMID:36215680[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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