Aerolysin

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Aerolysin
PDB 1pre EBI.jpg
proaerolysin
Identifiers
SymbolAerolysin
Pfam PF01117
Pfam clan CL0345
InterPro IPR005830
PROSITE PDOC00247
SCOP2 9fm6 1pre, 9fm6 / 9fm6 SCOPe / 9fm6 SUPFAM
TCDB 1.C.4
OPM superfamily 35
OPM protein 9fm6 5jzt, 9fm6
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

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]

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

  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. doi:10.1128/jb.169.6.2869-2871.1987. PMC   212202 . PMID   3584074.
  2. 1 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. doi:10.1038/367292a0. PMID   7510043. S2CID   4371932.
  3. 1 2 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. doi:10.1021/jacs.4c14288. PMC   11826888 .
  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.
  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.
  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. doi:10.1021/acssensors.8b01636. ISSN   2379-3694.
  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.
  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, doi:10.1101/2025.07.15.664886 , retrieved 2025-07-25
  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). doi:10.1038/s41467-018-03418-2. ISSN   2041-1723.
  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. doi:10.1021/acsnano.3c08623. ISSN   1936-0851.
  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). doi:10.1126/sciadv.abc2661. ISSN   2375-2548.
  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. doi:10.1021/acsnano.5b02096. ISSN   1936-0851.
  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). doi:10.1038/s41467-018-05108-5. ISSN   2041-1723.
  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.
  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, doi:10.1101/2025.01.13.632743 , retrieved 2025-07-25
  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). doi:10.1038/s41467-024-52674-y. ISSN   2041-1723.
  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. doi:10.1021/acs.nanolett.4c00035. ISSN   1530-6984.
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