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Cryo‐EM structure of the octameric pore of Clostridium perfringens β‐toxin
Open accessPublished version of a preprint
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 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.
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Metadata
- Authors
- Bruggisser, J., Iacovache, I., Musson, S. C., Degiacomi, M. T., Posthaus, H., & Zuber, B.
- Affiliations
- University of Bern (CH)
- Durham University (GB)
- Corresponding author
- Posthaus, Horst
- Zuber, Benoît
- ORCID
- Venue
- The EMBO Reports
- Published
- 2022-10-10
- Volume
- 23
- Issue
- 12
- Pages
- e54856-e54856
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC9724662
- OpenAlex
- W4304142251
- Cited by
- 13
- References
- 3
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 3 · 2023: 2 · 2022: 2
- FWCI
- 1.34
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- EMBO Reports (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Durham Research Online (Durham University) (acceptedVersion, other-oa)
- Durham Research Online (Durham University) (submittedVersion, cc-by)
- Bern Open Repository and Information System (University of Bern) (submittedVersion, cc-by)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, cc-by)
- Open Access CRIS of the University of Bern
- Funders
- Berne University Research Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (31003A_169381, 31003A_179520)
- UKRI¦Engineering and Physical Sciences Research Council (EP/P016499/1)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Clostridium difficile and Clostridium perfringens research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Physical Sciences › Engineering › Biomedical Engineering › Nanopore and Nanochannel Transport Studies
- Keywords
- toxin oligomerization, receptor-binding region, cap domain, nanotechnology
- MeSH terms
- Clostridium perfringens, Cryoelectron Microscopy
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