Aerolysin

Aerolysin

A 54 kD cytolytic toxin produced by Aeromonas hydrophila, a gram-negative bacterium which causes gastroenteritis and deep wound infections. Aerolysin binds to eukaryotic (host) cells and aggregates to form a ±3 nm in diameter transmembrane ion channel, leading to the destruction of the membrane permeability barrier and osmotic lysis.
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Gram positive bacteria, included Bacillus subtilis and Staphylococcus hominis cause diseases in severely immune-compromised patients, Bacillus cereus causes severe nausea, vomiting, and diarrhea, Bacillus anthracis leads to anthrax disease (30) Staphylococcus aureus causes scalded-skin syndrome (31), Streptococcus sanguis causes sub-acute bacterial endocarditis (32) and Aeromonas hydrophila produces aerolysin cytotoxic enterotoxin leads to tissue damage (9).
Virulence of Aeromonads is considered to be multifactorial including cytotonic heat-labile (alt), and cytotonic heat-stable enterotoxins (ast), cytotoxic heat-labile enterotoxin (act), hemolysin (hly), aerolysin (aei), flagella A and flagella B (fla), lipase (lip), elastase (ela), serine protease (ser), and DNases (exu) [8].
Cytotoxic enterotoxin, cytotonic enterotoxin and aerolysin play crucial roles in establishment of infections [21].
Aeromonas species can produce many virulence factors, including hemolysin, cytotoxin, aerolysin, enterotoxin, endotoxin, protease, adhesins, leukocidin, and lipases.
hydrophila produces several extracellular products such as proteases, haemolysins, aerolysin, cytolytic enterotoxins that are related with its pathogenicity (virulence) (Kingombe et al.
Previous studies have shown that production of hemolysin, aerolysin, cytolytic toxins and bacterial membrane receptors might individually contribute the virulence of A.
Differential regulation of caspase-1 activation via NLRP3/NLRC4 inflammasomes mediated by aerolysin and type III secretion system during Aeromonas veronii infection.
It is known that aerolysin, a PFT from Aeromonas hydrophila with structural and functional similarity to VCC, depends critically for its association with lipid rafts for insertion into the bilayer to generate a functional channel (23).
The possibility of anti-parallel [beta]-sheets being inserted into the lipid bilayer is demonstrated by the protease protection and analytical studies on diphtheria toxin, and aerolysin (Cabiaux et al, 1994; Parker et al, 1994).