{{Short description|Pore forming toxin}} {{Infobox protein family | Symbol = Aerolysin | Name = Aerolysin | image = Aerolysin gif.gif | width = | caption = Aerolysin | Pfam = PF01117 | Pfam_clan = CL0345 | InterPro = IPR005830 | SMART = | PROSITE = PDOC00247 | MEROPS = | SCOP = 1pre, 9fm6 | TCDB = 1.C.4 | OPM family = 35 | OPM protein = 5jzt, 9fm6 | CAZy = | CDD = }} 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.<ref name="pmid3584074">{{cite journal |vauthors=Howard SP, Garland WJ, Green MJ, Buckley JT | title = Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila | journal = J. Bacteriol. | volume = 169 | issue = 6 | pages = 2869–71 |date=June 1987 | pmid = 3584074 | pmc = 212202 | doi = 10.1128/jb.169.6.2869-2871.1987 | bibcode = 1987JBact.169.2869H }}</ref><ref name="pmid7510043">{{cite journal |vauthors=Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D | title = Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states | journal = Nature | volume = 367 | issue = 6460 | pages = 292–5 |date=January 1994 | pmid = 7510043 | doi = 10.1038/367292a0 | bibcode = 1994Natur.367..292P | s2cid = 4371932 }}</ref> 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.<ref name="pmid7510043"/> 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.<ref name=":0">{{cite journal |last1=Anton |first1=Jana S. |last2=Iacovache |first2=Ioan |last3=Bada Juarez |first3=Juan F. |last4=Abriata |first4=Luciano A. |last5=Perrin |first5=Louis W. |last6=Cao |first6=Chan |last7=Marcaida |first7=Maria J. |last8=Zuber |first8=Benoît |last9=Dal Peraro |first9=Matteo |title=Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment |journal=Journal of the American Chemical Society |date=12 February 2025 |volume=147 |issue=6 |pages=4984–4992 |doi=10.1021/jacs.4c14288|pmid=39900531 |pmc=11826888 |bibcode=2025JAChS.147.4984A }}</ref>
== Aerolysin as a biosensor == Aerolysin has also been used as a biosensor due to its narrow lumen and four constrictions points,<ref name=":0" /> which could be easily mutated, rendering aerolysin very sensitive<ref>{{Cite journal |last1=Zhang |first1=Yun |last2=Cao |first2=Chan |date=2025-02-26 |title=Aerolysin Nanopores for Single-Molecule Analysis |url=https://www.chimia.ch/chimia/article/view/2025_18 |journal=CHIMIA |volume=79 |issue=1–2 |pages=18–24 |doi=10.2533/chimia.2025.18 |issn=2673-2424|doi-access=free |pmid=40026087 }}</ref><ref>{{Cite journal |last1=Li |first1=Jun-Ge |last2=Ying |first2=Yi-Lun |last3=Long |first3=Yi-Tao |date=2025-02-18 |title=Aerolysin Nanopore Electrochemistry |url=https://pubs.acs.org/doi/10.1021/acs.accounts.4c00630 |journal=Accounts of Chemical Research |language=en |volume=58 |issue=4 |pages=517–528 |doi=10.1021/acs.accounts.4c00630 |pmid=39874057 |issn=0001-4842|url-access=subscription }}</ref><ref>{{Cite journal |last1=Cressiot |first1=Benjamin |last2=Ouldali |first2=Hadjer |last3=Pastoriza-Gallego |first3=Manuela |last4=Bacri |first4=Laurent |last5=Van der Goot |first5=F. Gisou |last6=Pelta |first6=Juan |date=2019-03-22 |title=Aerolysin, a Powerful Protein Sensor for Fundamental Studies and Development of Upcoming Applications |url=https://pubs.acs.org/doi/10.1021/acssensors.8b01636 |journal=ACS Sensors |language=en |volume=4 |issue=3 |pages=530–548 |doi=10.1021/acssensors.8b01636 |pmid=30747518 |bibcode=2019ACSSe...4..530C |issn=2379-3694}}</ref> for the detection of small molecules,<ref>{{Cite journal |last1=Boukhet |first1=Mordjane |last2=Piguet |first2=Fabien |last3=Ouldali |first3=Hadjer |last4=Pastoriza-Gallego |first4=Manuela |last5=Pelta |first5=Juan |last6=Oukhaled |first6=Abdelghani |date=2016 |title=Probing driving forces in aerolysin and α-hemolysin biological nanopores: electrophoresis versus electroosmosis |url=https://xlink.rsc.org/?DOI=C6NR06936C |journal=Nanoscale |language=en |volume=8 |issue=43 |pages=18352–18359 |doi=10.1039/C6NR06936C |pmid=27762420 |issn=2040-3364|url-access=subscription }}</ref> (cyclic<ref>{{cite bioRxiv |last1=Agerova |first1=Alissa |title=Sub-Nanomolar Detection and Discrimination of Microcystin Congeners Using Aerolysin Nanopores |date=2025-07-18 |language=en |biorxiv=10.1101/2025.07.15.664886 |last2=Bada Juarez |first2=Juan Francisco |last3=Abriata |first3=Luciano A. |last4=Marcaida |first4=Maria J. |last5=Carratalà |first5=Anna |last6=Janssen |first6=Elizabeth M. L. |last7=Cao |first7=Chan |last8=Kohn |first8=Tamar |last9=Dal Peraro |first9=Matteo}}</ref>) peptides,<ref>{{Cite journal |last1=Piguet |first1=Fabien |last2=Ouldali |first2=Hadjer |last3=Pastoriza-Gallego |first3=Manuela |last4=Manivet |first4=Philippe |last5=Pelta |first5=Juan |last6=Oukhaled |first6=Abdelghani |date=2018-03-06 |title=Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore |journal=Nature Communications |language=en |volume=9 |issue=1 |article-number=966 |doi=10.1038/s41467-018-03418-2 |pmid=29511176 |issn=2041-1723|pmc=5840376 |bibcode=2018NatCo...9..966P }}</ref><ref>{{Cite journal |last1=Cao |first1=Chan |last2=Magalhães |first2=Pedro |last3=Krapp |first3=Lucien F. |last4=Bada Juarez |first4=Juan F. |last5=Mayer |first5=Simon Finn |last6=Rukes |first6=Verena |last7=Chiki |first7=Anass |last8=Lashuel |first8=Hilal A. |last9=Dal Peraro |first9=Matteo |date=2024-01-16 |title=Deep Learning-Assisted Single-Molecule Detection of Protein Post-translational Modifications with a Biological Nanopore |journal=ACS Nano |language=en |volume=18 |issue=2 |pages=1504–1515 |doi=10.1021/acsnano.3c08623 |issn=1936-0851|pmc=10795472 |bibcode=2024ACSNa..18.1504C }}</ref> polymers,<ref>{{Cite journal |last1=Cao |first1=Chan |last2=Krapp |first2=Lucien F. |last3=Al Ouahabi |first3=Abdelaziz |last4=König |first4=Niklas F. |last5=Cirauqui |first5=Nuria |last6=Radenovic |first6=Aleksandra |last7=Lutz |first7=Jean-François |last8=Peraro |first8=Matteo Dal |date=2020-12-11 |title=Aerolysin nanopores decode digital information stored in tailored macromolecular analytes |journal=Science Advances |language=en |volume=6 |issue=50 |article-number=eabc2661 |doi=10.1126/sciadv.abc2661 |pmid=33298438 |issn=2375-2548|pmc=7725454 |bibcode=2020SciA....6.2661C }}</ref><ref>{{Cite journal |last1=Baaken |first1=Gerhard |last2=Halimeh |first2=Ibrahim |last3=Bacri |first3=Laurent |last4=Pelta |first4=Juan |last5=Oukhaled |first5=Abdelghani |last6=Behrends |first6=Jan C. |date=2015-06-23 |title=High-Resolution Size-Discrimination of Single Nonionic Synthetic Polymers with a Highly Charged Biological Nanopore |url=https://pubs.acs.org/doi/10.1021/acsnano.5b02096 |journal=ACS Nano |language=en |volume=9 |issue=6 |pages=6443–6449 |doi=10.1021/acsnano.5b02096 |pmid=26028280 |bibcode=2015ACSNa...9.6443B |issn=1936-0851|url-access=subscription }}</ref> biopolymers such as DNA<ref>{{Cite journal |last1=Cao |first1=Chan |last2=Li |first2=Meng-Yin |last3=Cirauqui |first3=Nuria |last4=Wang |first4=Ya-Qian |last5=Dal Peraro |first5=Matteo |last6=Tian |first6=He |last7=Long |first7=Yi-Tao |date=2018-07-19 |title=Mapping the sensing spots of aerolysin for single oligonucleotides analysis |journal=Nature Communications |language=en |volume=9 |issue=1 |article-number=2823 |doi=10.1038/s41467-018-05108-5 |issn=2041-1723|pmc=6053387 |bibcode=2018NatCo...9.2823C }}</ref> or RNA,<ref>{{Cite journal |last1=Yang |first1=Jie |last2=Wang |first2=Ya-Qian |last3=Li |first3=Meng-Yin |last4=Ying |first4=Yi-Lun |last5=Long |first5=Yi-Tao |date=2018-12-11 |title=Direct Sensing of Single Native RNA with a Single-Biomolecule Interface of Aerolysin Nanopore |url=https://pubs.acs.org/doi/10.1021/acs.langmuir.8b03264 |journal=Langmuir |language=en |volume=34 |issue=49 |pages=14940–14945 |doi=10.1021/acs.langmuir.8b03264 |pmid=30462509 |issn=0743-7463|url-access=subscription }}</ref> different sugars<ref>{{Cite journal |last1=Fennouri |first1=Aziz |last2=Ramiandrisoa |first2=Joana |last3=Bacri |first3=Laurent |last4=Mathé |first4=Jérôme |last5=Daniel |first5=Régis |date=October 2018 |title=Comparative biosensing of glycosaminoglycan hyaluronic acid oligo- and polysaccharides using aerolysin and α-hemolysin nanopores⋆ |url=http://link.springer.com/10.1140/epje/i2018-11733-5 |journal=The European Physical Journal E |language=en |volume=41 |issue=10 |doi=10.1140/epje/i2018-11733-5 |issn=1292-8941}}</ref> and also some proteins.<ref>{{cite bioRxiv |last1=Rukes |first1=Verena |title=Charge-based fingerprinting of unlabeled full-length proteins using an aerolysin nanopore |date=2025-01-16 |language=en |biorxiv=10.1101/2025.01.13.632743 |last2=Norkute |first2=Evita |last3=Barnikol |first3=Georges |last4=Duan |first4=Jingze |last5=Gao |first5=Jiajie |last6=Cao |first6=Chan}}</ref>
Aerolysin has also been used as a tool to assess the action mechanism of the Hsp70 protein<ref>{{Cite journal |last1=Rukes |first1=Verena |last2=Rebeaud |first2=Mathieu E. |last3=Perrin |first3=Louis W. |last4=De Los Rios |first4=Paolo |last5=Cao |first5=Chan |date=2024-10-08 |title=Single-molecule evidence of Entropic Pulling by Hsp70 chaperones |journal=Nature Communications |language=en |volume=15 |issue=1 |article-number=8604 |doi=10.1038/s41467-024-52674-y |pmid=39379347 |issn=2041-1723|pmc=11461734 |bibcode=2024NatCo..15.8604R }}</ref> 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.<ref>{{Cite journal |last1=Roesel |first1=Tereza |last2=Cao |first2=Chan |last3=Bada Juarez |first3=Juan F. |last4=Dal Peraro |first4=Matteo |last5=Roke |first5=Sylvie |date=2024-11-06 |title=Dissecting the Membrane Association Mechanism of Aerolysin Pores at Femtomolar Concentrations Using Water as a Probe |journal=Nano Letters |language=en |volume=24 |issue=44 |pages=13888–13894 |doi=10.1021/acs.nanolett.4c00035 |issn=1530-6984|pmc=11544699 |bibcode=2024NanoL..2413888R }}</ref>
==References== {{reflist}} {{InterPro content|IPR005830}}
Category:Protein domains