{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bruggisser J"],"funding":["Stavros Niarchos Foundation","Swiss National Science Foundation","Engineering and Physical Sciences Research Council"],"pagination":["e54856"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9724662"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(12)"],"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 s"],"journal":["EMBO reports"],"pubmed_title":["Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin."],"pmcid":["PMC9724662"],"funding_grant_id":["EP/P016499/1","169381","31003A_169381","31003A_179520","179520"],"pubmed_authors":["Posthaus H","Iacovache I","Zuber B","Degiacomi MT","Bruggisser J","Musson SC"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin.","description":"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 s","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-10T06:52:00.627Z","creation":"2025-02-19T03:26:18.865Z"},"accession":"S-EPMC9724662","cross_references":{"pubmed":["36215680"],"doi":["10.15252/embr.202254856"]}}