Aerolysin [ (PUBMED:3584074) ] is a cytolytic toxin exported by Aeromonas hydrophila, a Gram-negative bacterium associated with diarrhoeal diseases and deep wound infections [ (PUBMED:7510043) ]. 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 [ (PUBMED:7510043) ]. Images of an aerolysin oligomer derived from electron microscopy have helped to construct a model of the protein and to outline a mechanism by which it might insert into lipid bilayers to form ion channels [ (PUBMED:7510043) ].
Structure of the Aeromonas toxin proaerolysin in its water-soluble andmembrane-channel states.
Nature. 1994; 367: 292-5
Display abstract
Aerolysin is chiefly responsible for the pathogenicity of Aeromonashydrophila, a bacterium associated with diarrhoeal diseases and deep woundinfections. Like many other microbial toxins, the protein changes in amultistep process from a completely water-soluble form to produce atransmembrane channel that destroys sensitive cells by breaking theirpermeability barriers. Here we describe the structure of proaerolysindetermined by X-ray crystallography at 2.8 A resolution. The protoxin(M(r) 52,000) adopts a novel protein fold. Images of an aerolysin oligomerderived from electron microscopy have assisted in constructing a model ofthe membrane channel and have led to the proposal of a scheme to accountfor insertion of the protein into lipid bilayers to form ion channels.
Nucleotide sequence of the gene for the hole-forming toxin aerolysin ofAeromonas hydrophila.
J Bacteriol. 1987; 169: 2869-71
Display abstract
The gene for the hole-forming toxin aerolysin from Aeromonas hydrophilawas sequenced. Although most of the sequence seems unrelated to that ofStaphylococcus aureus alpha-toxin, both proteins are very hydrophilic, andthey each contain a nearly identical string of 10 amino acids.
