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Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin

Julia Bruggisser, View ORCID ProfileIoan Iacovache, View ORCID ProfileSamuel C. Musson, View ORCID ProfileMatteo T. Degiacomi, View ORCID ProfileHorst Posthaus, View ORCID ProfileBenoît Zuber
doi: https://doi.org/10.1101/2021.11.23.469684
Julia Bruggisser
1Institute of Animal Pathology, Vetsuisse-Faculty, University of Bern, Switzerland
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Ioan Iacovache
2Institute of Anatomy, Medical Faculty, University of Bern, Switzerland
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Samuel C. Musson
3Department of Physics, Durham University, U.K
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Matteo T. Degiacomi
3Department of Physics, Durham University, U.K
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Horst Posthaus
1Institute of Animal Pathology, Vetsuisse-Faculty, University of Bern, Switzerland
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  • For correspondence: benoit.zuber@unibe.ch
Benoît Zuber
2Institute of Anatomy, Medical Faculty, University of Bern, Switzerland
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  • For correspondence: benoit.zuber@unibe.ch
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ABSTRACT

We describe the cryo-EM structure of Clostridium perfringens β-toxin (CBP) in styrene maleic acid (SMA) discs, which represents the membrane-inserted pore form, at near atomic resolution. We show that CPB forms an octamer, which though having a similar conformation to the hetero-oligomeric pores of bicomponent leukocidins, features a different receptor binding region and a novel N-terminal β-barrel. The latter contains an additional selectivity filter and creates a bipolar pore. We propose that the N-terminal β-barrel domain may regulate oligomerization and solubility of the complex and influence channel conductance and monomer stability. In addition, we show that the β-barrel protrusion domain can be modified or exchanged 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.

Competing Interest Statement

The authors have declared no competing interest.

  • ABBREVIATIONS

    CPB
    C. perfringens β-toxin
    SMA
    styrene maleic acid
    PFT
    pore forming toxin
    NBP
    N-terminal β-barrel protrusion
    PMF
    potential mean force
    RMSF
    root mean square fluctuation
  • Copyright 
    The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-ND 4.0 International license.
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    Posted November 23, 2021.
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    Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin
    Julia Bruggisser, Ioan Iacovache, Samuel C. Musson, Matteo T. Degiacomi, Horst Posthaus, Benoît Zuber
    bioRxiv 2021.11.23.469684; doi: https://doi.org/10.1101/2021.11.23.469684
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    Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin
    Julia Bruggisser, Ioan Iacovache, Samuel C. Musson, Matteo T. Degiacomi, Horst Posthaus, Benoît Zuber
    bioRxiv 2021.11.23.469684; doi: https://doi.org/10.1101/2021.11.23.469684

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