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Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly

Author

Listed:
  • Marjetka Podobnik

    (National Institute of Chemistry)

  • Peter Savory

    (Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park)

  • Nejc Rojko

    (National Institute of Chemistry)

  • Matic Kisovec

    (National Institute of Chemistry)

  • Neil Wood

    (Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park)

  • Richard Hambley

    (Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park)

  • Jonathan Pugh

    (Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park)

  • E. Jayne Wallace

    (Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park)

  • Luke McNeill

    (Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park)

  • Mark Bruce

    (Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park)

  • Idlir Liko

    (University of Oxford)

  • Timothy M. Allison

    (University of Oxford)

  • Shahid Mehmood

    (University of Oxford)

  • Neval Yilmaz

    (Lipid Biology Laboratory, RIKEN Institute)

  • Toshihide Kobayashi

    (Lipid Biology Laboratory, RIKEN Institute)

  • Robert J. C. Gilbert

    (Wellcome Trust Centre for Human Genetics, University of Oxford)

  • Carol V. Robinson

    (University of Oxford)

  • Lakmal Jayasinghe

    (Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park)

  • Gregor Anderluh

    (National Institute of Chemistry)

Abstract

The invertebrate cytolysin lysenin is a member of the aerolysin family of pore-forming toxins that includes many representatives from pathogenic bacteria. Here we report the crystal structure of the lysenin pore and provide insights into its assembly mechanism. The lysenin pore is assembled from nine monomers via dramatic reorganization of almost half of the monomeric subunit structure leading to a β-barrel pore ∼10 nm long and 1.6–2.5 nm wide. The lysenin pore is devoid of additional luminal compartments as commonly found in other toxin pores. Mutagenic analysis and atomic force microscopy imaging, together with these structural insights, suggest a mechanism for pore assembly for lysenin. These insights are relevant to the understanding of pore formation by other aerolysin-like pore-forming toxins, which often represent crucial virulence factors in bacteria.

Suggested Citation

  • Marjetka Podobnik & Peter Savory & Nejc Rojko & Matic Kisovec & Neil Wood & Richard Hambley & Jonathan Pugh & E. Jayne Wallace & Luke McNeill & Mark Bruce & Idlir Liko & Timothy M. Allison & Shahid Me, 2016. "Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly," Nature Communications, Nature, vol. 7(1), pages 1-10, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11598
    DOI: 10.1038/ncomms11598
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    Cited by:

    1. 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.

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