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Nat Commun. 2016 May 12;7:11598. doi: 10.1038/ncomms11598.

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

Author information

1
Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
2
Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park, Oxford OX4 4GA, UK.
3
Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
4
Lipid Biology Laboratory, RIKEN Institute, Wako 351-0198, Japan.
5
Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.

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.

PMID:
27176125
PMCID:
PMC4865846
DOI:
10.1038/ncomms11598
[Indexed for MEDLINE]
Free PMC Article

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