Aerolysin

{{Infobox protein family

| Symbol = Aerolysin

| Name = Aerolysin

| image = PDB 1pre EBI.jpg

| width =

| caption = proaerolysin

| Pfam = PF01117

| Pfam_clan = CL0345

| InterPro = IPR005830

| SMART =

| PROSITE = PDOC00247

| MEROPS =

| SCOP = 1pre

| TCDB = 1.C.4

| OPM family = 35

| OPM protein = 5jzt

| 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.{{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}}{{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 | s2cid = 4371932 }} 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.{{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 | s2cid = 4371932 }} 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. {{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|pmc=11826888 }}