ArticleNature communications2016
Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 93 citations in OpenAlex.
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- Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by CuInternational journal of molecular sciences · 2023Article
- Hypo-Osmotic Stress and Pore-Forming Toxins Adjust the Lipid Order in Sheep Red Blood Cell Membranes.Membranes · 2023Article
- An oomycete NLP cytolysin forms transient small pores in lipid membranes.Science advances · 2022Article
- Article
- Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer.The Journal of cell biology · 2021Article
- A high-throughput predictive method for sequence-similar fold switchers.Biopolymers · 2021Article
- A sequence-based method for predicting extant fold switchers that undergo α-helix ↔ β-strand transitions.Biopolymers · 2021Article
- Beyond pore formation: reorganization of the plasma membrane induced by pore-forming proteins.Cellular and molecular life sciences : CMLS · 2021Review
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Authors and funding
19 authors at 5 institutions in 4 countries.
Funding
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.
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