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