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Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein

Author

Listed:
  • Monika Bokori-Brown

    (Biosciences, College of Life and Environmental Sciences, University of Exeter)

  • Thomas G. Martin

    (MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus)

  • Claire E. Naylor

    (Birkbeck College)

  • Ajit K. Basak

    (Birkbeck College)

  • Richard W. Titball

    (Biosciences, College of Life and Environmental Sciences, University of Exeter)

  • Christos G. Savva

    (MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus)

Abstract

Lysenin from the coelomic fluid of the earthworm Eisenia fetida belongs to the aerolysin family of small β-pore-forming toxins (β-PFTs), some members of which are pathogenic to humans and animals. Despite efforts, a high-resolution structure of a channel for this family of proteins has been elusive and therefore the mechanism of activation and membrane insertion remains unclear. Here we determine the pore structure of lysenin by single particle cryo-EM, to 3.1 Å resolution. The nonameric assembly reveals a long β-barrel channel spanning the length of the complex that, unexpectedly, includes the two pre-insertion strands flanking the hypothetical membrane-insertion loop. Examination of other members of the aerolysin family reveals high structural preservation in this region, indicating that the membrane-insertion pathway in this family is conserved. For some toxins, proteolytic activation and pro-peptide removal will facilitate unfolding of the pre-insertion strands, allowing them to form the β-barrel of the channel.

Suggested Citation

  • Monika Bokori-Brown & Thomas G. Martin & Claire E. Naylor & Ajit K. Basak & Richard W. Titball & Christos G. Savva, 2016. "Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein," Nature Communications, Nature, vol. 7(1), pages 1-7, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11293
    DOI: 10.1038/ncomms11293
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    1. Ivica Odorčić & Mohamed Belal Hamed & Sam Lismont & Lucía Chávez-Gutiérrez & Rouslan G. Efremov, 2024. "Apo and Aβ46-bound γ-secretase structures provide insights into amyloid-β processing by the APH-1B isoform," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Jiaqiang Zhu & Wei Huang & Jing Zhao & Loc Huynh & Derek J. Taylor & Michael E. Harris, 2022. "Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Nario Tomishige & Maaz Nasim & Motohide Murate & Brigitte Pollet & Pascal Didier & Julien Godet & Ludovic Richert & Yasushi Sako & Yves Mély & Toshihide Kobayashi, 2023. "HIV-1 Gag targeting to the plasma membrane reorganizes sphingomyelin-rich and cholesterol-rich lipid domains," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    4. Guendalina Marini & Brad Poland & Chris Leininger & Natalya Lukoyanova & Dan Spielbauer & Jennifer K. Barry & Dan Altier & Amy Lum & Eric Scolaro & Claudia Pérez Ortega & Nasser Yalpani & Gary Sandahl, 2023. "Structural journey of an insecticidal protein against western corn rootworm," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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