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Aerolysin

Pore forming toxin

Field	Value
Symbol	Aerolysin
Name	Aerolysin
image	Aerolysin gif.gif
caption	Aerolysin
Pfam	PF01117
Pfam_clan	CL0345
InterPro	IPR005830
PROSITE	PDOC00247
SCOP	1pre, 9fm6
TCDB	1.C.4
OPM family	35
OPM protein	5jzt, 9fm6

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. 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. 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.

Aerolysin as a biosensor

Aerolysin has also been used as a biosensor due to its narrow lumen and four constrictions points, which could be easily mutated, rendering aerolysin very sensitive for the detection of small molecules, (cyclic) peptides, polymers, biopolymers such as DNA or RNA, different sugars and also some proteins.

Aerolysin has also been used as a tool to assess the action mechanism of the Hsp70 protein 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.

References

(June 1987). "Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila". J. Bacteriol..
(January 1994). "Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states". Nature.
(12 February 2025). "Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment". Journal of the American Chemical Society.
(2025-02-26). "Aerolysin Nanopores for Single-Molecule Analysis". CHIMIA.
(2025-02-18). "Aerolysin Nanopore Electrochemistry". Accounts of Chemical Research.
(2019-03-22). "Aerolysin, a Powerful Protein Sensor for Fundamental Studies and Development of Upcoming Applications". ACS Sensors.
(2016). "Probing driving forces in aerolysin and α-hemolysin biological nanopores: electrophoresis versus electroosmosis". Nanoscale.
(2025-07-18). "Sub-Nanomolar Detection and Discrimination of Microcystin Congeners Using Aerolysin Nanopores".
(2018-03-06). "Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore". Nature Communications.
(2024-01-16). "Deep Learning-Assisted Single-Molecule Detection of Protein Post-translational Modifications with a Biological Nanopore". ACS Nano.
(2020-12-11). "Aerolysin nanopores decode digital information stored in tailored macromolecular analytes". Science Advances.
(2015-06-23). "High-Resolution Size-Discrimination of Single Nonionic Synthetic Polymers with a Highly Charged Biological Nanopore". ACS Nano.
(2018-07-19). "Mapping the sensing spots of aerolysin for single oligonucleotides analysis". Nature Communications.
(2018-12-11). "Direct Sensing of Single Native RNA with a Single-Biomolecule Interface of Aerolysin Nanopore". Langmuir.
(October 2018). "Comparative biosensing of glycosaminoglycan hyaluronic acid oligo- and polysaccharides using aerolysin and α-hemolysin nanopores⋆". The European Physical Journal E.
(2025-01-16). "Charge-based fingerprinting of unlabeled full-length proteins using an aerolysin nanopore".
(2024-10-08). "Single-molecule evidence of Entropic Pulling by Hsp70 chaperones". Nature Communications.
(2024-11-06). "Dissecting the Membrane Association Mechanism of Aerolysin Pores at Femtomolar Concentrations Using Water as a Probe". Nano Letters.

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