Aerolysin

Pore forming toxin From Wikipedia, the free encyclopedia

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]

Quick facts Identifiers, Symbol ...
Aerolysin
Aerolysin
Identifiers
SymbolAerolysin
PfamPF01117
Pfam clanCL0345
InterProIPR005830
PROSITEPDOC00247
SCOP29fm6 1pre, 9fm6 / 9fm6 SCOPe / 9fm6 SUPFAM
TCDB1.C.4
OPM superfamily35
OPM protein9fm6 5jzt, 9fm6
Available protein structures:
PDB  IPR005830 PF01117 (ECOD; PDBsum)  
AlphaFold
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Aerolysin as a biosensor

Aerolysin has also been used as a biosensor due to its narrow lumen and four constrictions points,[3] which could be easily mutated, rendering aerolysin very sensitive[4][5][6] for the detection of small molecules,[7] (cyclic[8]) peptides,[9][10] polymers,[11][12] biopolymers such as DNA[13] or RNA,[14] different sugars[15] and also some proteins.[16]

Aerolysin has also been used as a tool to assess the action mechanism of the Hsp70 protein[17] and to study the association mechanism to the membrane as well as pore formation with angle-resolved second harmonic scattering (AR-SHS), enabling to quantify quantitatively the affinity of aerolysin to lipids using liposomes.[18]

References

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