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Aerolysin
proaerolysin
Identifiers
Symbol	Aerolysin
Pfam	PF01117
Pfam clan	CL0345
InterPro	IPR005830
PROSITE	PDOC00247
SCOP2	1pre / SCOPe / SUPFAM
TCDB	1.C.4
OPM superfamily	35
OPM protein	5jzt
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. 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. Images of an aerolysin oligomer derived from electron microscopy have helped to construct a model of the protein in its heptameric conformation, and to outline a mechanism by which this assembly might insert into lipid bilayers to form ion channels.

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. ^ 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. Degiacomi MT, Iacovache I, Pernot L, Chami M, Kudryashev M, Stahlberg H, van der Goot FG, Dal Peraro M (August 2013). "Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism. The gene for aerolysin have been shown to undergo Horizontal gene transfer from prokaryotes to eukaryotes" (PDF). Nature Chemical Biology. 9 (6460): 623–629. doi:10.1038/nchembio.1312. PMID 23912165.

• Protein domains