Article · Wikipedia archive · Last revised Jun 9, 2026

Aerolysin

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 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 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.

Last revised
Jun 9, 2026
Read time
≈ 4 min
Length
920 w
Citations
20
Source
Wikipedia ↗
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

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.12 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

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 sensitive456 for the detection of small molecules,7 (cyclic8) peptides,910 polymers,1112 biopolymers such as DNA13 or RNA,14 different sugars15 and also some proteins.16

Aerolysin has also been used as a tool to assess the action mechanism of the Hsp70 protein17 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

References

  1. Howard SP, Garland WJ, Green MJ, Buckley JT (June 1987). "Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila". J. Bacteriol. 169 (6): 2869–71. Bibcode:1987JBact.169.2869H. doi:10.1128/jb.169.6.2869-2871.1987. PMC 212202. PMID 3584074.
  2. Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D (January 1994). "Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states". Nature. 367 (6460): 292–5. Bibcode:1994Natur.367..292P. doi:10.1038/367292a0. PMID 7510043. S2CID 4371932.
  3. Anton, Jana S.; Iacovache, Ioan; Bada Juarez, Juan F.; Abriata, Luciano A.; Perrin, Louis W.; Cao, Chan; Marcaida, Maria J.; Zuber, Benoît; Dal Peraro, Matteo (12 February 2025). "Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment". Journal of the American Chemical Society. 147 (6): 4984–4992. Bibcode:2025JAChS.147.4984A. doi:10.1021/jacs.4c14288. PMC 11826888. PMID 39900531.
  4. Zhang, Yun; Cao, Chan (2025-02-26). "Aerolysin Nanopores for Single-Molecule Analysis". CHIMIA. 79 (1–2): 18–24. doi:10.2533/chimia.2025.18. ISSN 2673-2424. PMID 40026087.
  5. Li, Jun-Ge; Ying, Yi-Lun; Long, Yi-Tao (2025-02-18). "Aerolysin Nanopore Electrochemistry". Accounts of Chemical Research. 58 (4): 517–528. doi:10.1021/acs.accounts.4c00630. ISSN 0001-4842. PMID 39874057.
  6. Cressiot, Benjamin; Ouldali, Hadjer; Pastoriza-Gallego, Manuela; Bacri, Laurent; Van der Goot, F. Gisou; Pelta, Juan (2019-03-22). "Aerolysin, a Powerful Protein Sensor for Fundamental Studies and Development of Upcoming Applications". ACS Sensors. 4 (3): 530–548. Bibcode:2019ACSSe...4..530C. doi:10.1021/acssensors.8b01636. ISSN 2379-3694. PMID 30747518.
  7. Boukhet, Mordjane; Piguet, Fabien; Ouldali, Hadjer; Pastoriza-Gallego, Manuela; Pelta, Juan; Oukhaled, Abdelghani (2016). "Probing driving forces in aerolysin and α-hemolysin biological nanopores: electrophoresis versus electroosmosis". Nanoscale. 8 (43): 18352–18359. doi:10.1039/C6NR06936C. ISSN 2040-3364. PMID 27762420.
  8. Agerova, Alissa; Bada Juarez, Juan Francisco; Abriata, Luciano A.; Marcaida, Maria J.; Carratalà, Anna; Janssen, Elizabeth M. L.; Cao, Chan; Kohn, Tamar; Dal Peraro, Matteo (2025-07-18). "Sub-Nanomolar Detection and Discrimination of Microcystin Congeners Using Aerolysin Nanopores". bioRxiv 10.1101/2025.07.15.664886.
  9. Piguet, Fabien; Ouldali, Hadjer; Pastoriza-Gallego, Manuela; Manivet, Philippe; Pelta, Juan; Oukhaled, Abdelghani (2018-03-06). "Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore". Nature Communications. 9 (1) 966. Bibcode:2018NatCo...9..966P. doi:10.1038/s41467-018-03418-2. ISSN 2041-1723. PMC 5840376. PMID 29511176.
  10. Cao, Chan; Magalhães, Pedro; Krapp, Lucien F.; Bada Juarez, Juan F.; Mayer, Simon Finn; Rukes, Verena; Chiki, Anass; Lashuel, Hilal A.; Dal Peraro, Matteo (2024-01-16). "Deep Learning-Assisted Single-Molecule Detection of Protein Post-translational Modifications with a Biological Nanopore". ACS Nano. 18 (2): 1504–1515. Bibcode:2024ACSNa..18.1504C. doi:10.1021/acsnano.3c08623. ISSN 1936-0851. PMC 10795472.
  11. Cao, Chan; Krapp, Lucien F.; Al Ouahabi, Abdelaziz; König, Niklas F.; Cirauqui, Nuria; Radenovic, Aleksandra; Lutz, Jean-François; Peraro, Matteo Dal (2020-12-11). "Aerolysin nanopores decode digital information stored in tailored macromolecular analytes". Science Advances. 6 (50) eabc2661. Bibcode:2020SciA....6.2661C. doi:10.1126/sciadv.abc2661. ISSN 2375-2548. PMC 7725454. PMID 33298438.
  12. Baaken, Gerhard; Halimeh, Ibrahim; Bacri, Laurent; Pelta, Juan; Oukhaled, Abdelghani; Behrends, Jan C. (2015-06-23). "High-Resolution Size-Discrimination of Single Nonionic Synthetic Polymers with a Highly Charged Biological Nanopore". ACS Nano. 9 (6): 6443–6449. Bibcode:2015ACSNa...9.6443B. doi:10.1021/acsnano.5b02096. ISSN 1936-0851. PMID 26028280.
  13. Cao, Chan; Li, Meng-Yin; Cirauqui, Nuria; Wang, Ya-Qian; Dal Peraro, Matteo; Tian, He; Long, Yi-Tao (2018-07-19). "Mapping the sensing spots of aerolysin for single oligonucleotides analysis". Nature Communications. 9 (1) 2823. Bibcode:2018NatCo...9.2823C. doi:10.1038/s41467-018-05108-5. ISSN 2041-1723. PMC 6053387.
  14. Yang, Jie; Wang, Ya-Qian; Li, Meng-Yin; Ying, Yi-Lun; Long, Yi-Tao (2018-12-11). "Direct Sensing of Single Native RNA with a Single-Biomolecule Interface of Aerolysin Nanopore". Langmuir. 34 (49): 14940–14945. doi:10.1021/acs.langmuir.8b03264. ISSN 0743-7463. PMID 30462509.
  15. Fennouri, Aziz; Ramiandrisoa, Joana; Bacri, Laurent; Mathé, Jérôme; Daniel, Régis (October 2018). "Comparative biosensing of glycosaminoglycan hyaluronic acid oligo- and polysaccharides using aerolysin and α-hemolysin nanopores⋆". The European Physical Journal E. 41 (10). doi:10.1140/epje/i2018-11733-5. ISSN 1292-8941.
  16. Rukes, Verena; Norkute, Evita; Barnikol, Georges; Duan, Jingze; Gao, Jiajie; Cao, Chan (2025-01-16). "Charge-based fingerprinting of unlabeled full-length proteins using an aerolysin nanopore". bioRxiv 10.1101/2025.01.13.632743.
  17. Rukes, Verena; Rebeaud, Mathieu E.; Perrin, Louis W.; De Los Rios, Paolo; Cao, Chan (2024-10-08). "Single-molecule evidence of Entropic Pulling by Hsp70 chaperones". Nature Communications. 15 (1) 8604. Bibcode:2024NatCo..15.8604R. doi:10.1038/s41467-024-52674-y. ISSN 2041-1723. PMC 11461734. PMID 39379347.
  18. Roesel, Tereza; Cao, Chan; Bada Juarez, Juan F.; Dal Peraro, Matteo; Roke, Sylvie (2024-11-06). "Dissecting the Membrane Association Mechanism of Aerolysin Pores at Femtomolar Concentrations Using Water as a Probe". Nano Letters. 24 (44): 13888–13894. Bibcode:2024NanoL..2413888R. doi:10.1021/acs.nanolett.4c00035. ISSN 1530-6984. PMC 11544699.
This article incorporates text from the public domain Pfam and InterPro: IPR005830