Aerolysin

Overview:

The aerolysins are a closely related group of channel-forming toxins secreted by members of the family Aeromonas, important human and animal pathogens. They are activated by host and bacterial proteases which remove a C-terminal fragment of about 40 amino acyl residues. The activated monomeric toxin then binds to a receptor glycosyl phosphatidylinositol (GPI)-anchored protein on the surface of the target cell.

Data Sheet:

Gene:
aerA

Protein
UniProt: P09167 (Aeromonas hydrophila)

Topology:
Homodimer in solution; homoheptamer in the host membrane.

Function:
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. Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane.

Assays:
Bilayer Recordings on the Orbit Product family

Recommended Reviews:

• Podobnik et al.: Molecular mechanism of pore formation by aerolysin-like proteins (2017) Philos Trans R Soc Lond B Biol Sci. doi: 10.1098/rstb.2016.0209

Transporter classification database:

• 1.C.4 The Aerolysin Channel-forming Toxin (Aerolysin) Family

UniProt:

• Aerolysin (aerA, Aeromonas hydrophila)