Aerolysin
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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. It is also produced by the caterpillar of the moth Megalopyge opercularis, sometimes called the Tree Asp. 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. High-resolution cryo-EM atomic models of aerolysin in membrane-like environment (lipid copolymer Nanodiscs) as well as some prepore-like mutant have been elucidated, permitting the identification of important interactions required for pore formation and revealing four constriction rings in the pore lumen.
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. It is also produced by the caterpillar of the moth Megalopyge opercularis, sometimes called the Tree Asp. 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. High-resolution cryo-EM atomic models of aerolysin in membrane-like environment (lipid copolymer Nanodiscs) as well as some prepore-like mutant have been elucidated, permitting the identification of important interactions required for pore formation and revealing four constriction rings in the pore lumen.
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Text derived from https://en.wikipedia.org/w/index.php?oldid=1373648838 under CC BY-SA 4.0; modifications have been made.