• Aerolysin

    Screenshot s of a typical channel forming aerolysin activity assay with the Orbit 16.


Pore-forming Toxins

Members of this family are proteins/peptides, synthesized by one cell and secreted for insertion into the membrane of another cell where they form transmembrane pores. Pore-forming toxins (PFTs) are the most common bacterial cytotoxic proteins and are required for virulence in a large number of important pathogens.

Over 100 subgroups belong to the "Pore-forming Toxins" family, including amongst others:

  • The α-Hemolysin Channel-forming Toxin (αHL) Family
  • The Aerolysin Channel-forming Toxin (Aerolysin) Family
  • The Botulinum and Tetanus Toxin (BTT) Family
  • The Pertussis Toxin (PTX) Family
  • The Crystal Protein (Cry) Family

Aerolysin Background Information


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:


UniProt: P09167 (Aeromonas hydrophila)

Homodimer in solution; homoheptamer in the host membrane.

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.

Bilayer Recordings on the Orbit Product family

Reviews and Links



2022 - A Two-Step Calibration Method for Evaluation High Bandwidth Electrochemical Instrument

Icon Orbit  Orbit 16 publication in Journal of Electroanalytical Chemistry (2022)

Zhang L.L., Zhong C.B., Li J.G., Niu H.Y., Ying Y.L., Long Y.T.

2020 - Electrical recognition of the twenty proteinogenic amino acids using an aerolysin nanopore

Icon Orbit  Orbit 16 publication in Nature Biotechnology (2020)

Ouldali H., Sarthak K., Ensslen T., Piguet F., Manivet P., Pelta J., Behrends J.C., Aksimentiev A., Oukhaled A.

2020 - Aerolysin nanopores decode digital information stored in tailored macromolecular analytes

Icon Orbit Mini   Orbit mini publication in Science Advances (2020)

Cao C., Krapp L.F., Al Ouahabi A., König N.F., Cirauqui N., Radenovic A., Lutz J.F. Dal Peraro M.

2019 - A comparison of ion channel current blockades caused by individual poly(ethylene glycol) molecules and polyoxometalate nanoclusters

Icon Orbit   Orbit 16 publication in The European Physical Journal E (2019)

Wang H., Kasianowicz J.J., Robertson J.W.F., Poster D.L., Ettedgui J.

2018 - Size-dependent interaction of a 3-arm star poly(ethylene glycol) with two biological nanopores

Icon Orbit   Orbit 16 publication in The European Physical Journal E (2018)

Talarimoghari M., Baaken G., Hanselmann R., Behrends J.C.

2016 - Probing driving forces in aerolysin and α-hemolysin biological nanopores: electrophoresis versus electroosmosis

Icon Orbit  Orbit 16 publication in Nanoscale (2016)

Boukhet M., Piguet F., Ouldali H., Pastoriza-Gallego M., Pelta J., Oukhaled A.

2015 - High-Resolution Size-Discrimination of Single Nonionic Synthetic Polymers with a Highly Charged Biological Nanopore

Icon Orbit  Orbit 16 and   icon vpp   Vesicle Prep Pro publication in American Chemical Society Nano (2015)

Baaken G., Halimeh I., Bacri, Pelta J., Oukhaled A., Behrends J.C.


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