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-Structure paper
タイトル | Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin. |
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ジャーナル・号・ページ | EMBO Rep, Vol. 23, Issue 12, Page e54856, Year 2022 |
掲載日 | 2022年12月6日 |
著者 | Julia Bruggisser / Ioan Iacovache / Samuel C Musson / Matteo T Degiacomi / Horst Posthaus / Benoît Zuber / |
PubMed 要旨 | 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 ...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. |
リンク | EMBO Rep / PubMed:36215680 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.84 Å |
構造データ | EMDB-13876, PDB-7q9y: |
由来 |
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キーワード | TOXIN / pore forming toxin / hemolysin / octamer |