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

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 Mehmood, Neval Yilmaz, Toshihide Kobayashi, Robert J. C. Gilbert, Carol V. Robinson, Lakmal Jayasinghe () and Gregor Anderluh ()
Additional contact information
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

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms11598

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