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In molecular biology, aerolysin is a cytolytic pore-forming toxin exported by Aeromonas hydrophila , a Gram-negative bacterium associated with diarrhoeal diseases and deep wound infections .[ 1] [ 2] The mature toxin binds to eukaryotic cells and aggregates to form holes (approximately 3 nm in diameter) leading to the destruction of the membrane permeability barrier and osmotic lysis . The structure of proaerolysin has been determined to 2.8A resolution and shows the protoxin to adopt a novel fold .[ 2] Images of an aerolysin oligomer derived from electron microscopy and molecular dynamics simulations have helped to construct a model of the protein in its heptameric conformation, and to outline a mechanism by which this assembly might insert into lipid bilayers to form ion channels .[ 3]
References
^ Howard SP, Garland WJ, Green MJ, Buckley JT (June 1987). "Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila" . J. Bacteriol . 169 (6): 2869–71. PMC 212202 . PMID 3584074 .
^ a b Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D (January 1994). "Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states". Nature . 367 (6460): 292–5. doi :10.1038/367292a0 . PMID 7510043 .
^ Degiacomi MT, Iacovache I, Pernot L, Chami M, Kudryashev M, Stahlberg H, van der Goot FG, Dal Peraro M (August 2013). "Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism. The gene for aerolysin have been shown to undergo Horizontal gene transfer from prokaryotes to eukaryotes" . Nature Chemical Biology . 9 (6460): 623–629. doi :10.1038/nchembio.1312 . PMID 23912165 .