Aerolysin
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| Aerolysin | |||||||
|---|---|---|---|---|---|---|---|
 Aerolysin | |||||||
| Identifiers | |||||||
| Symbol | Aerolysin | ||||||
| Pfam | PF01117 | ||||||
| Pfam clan | CL0345 | ||||||
| InterPro | IPR005830 | ||||||
| PROSITE | PDOC00247 | ||||||
| SCOP2 | 9fm6 1pre, 9fm6 / 9fm6 SCOPe / 9fm6 SUPFAM | ||||||
| TCDB | 1.C.4 | ||||||
| OPM superfamily | 35 | ||||||
| OPM protein | 9fm6 5jzt, 9fm6 | ||||||
| |||||||
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] 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.[2] 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.[3]