Aerolysin Explained

Symbol:Aerolysin
Aerolysin
Pfam:PF01117
Pfam Clan:CL0345
Interpro:IPR005830
Prosite:PDOC00247
Scop:1pre
Tcdb:1.C.4
Opm Family:35
Opm Protein:5jzt

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.[3] 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.[4]

Notes and References

  1. Howard SP, Garland WJ, Green MJ, Buckley JT . Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila . J. Bacteriol. . 169 . 6 . 2869–71 . June 1987 . 3584074 . 212202 . 10.1128/jb.169.6.2869-2871.1987.
  2. Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D . Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states . Nature . 367 . 6460 . 292–5 . January 1994 . 7510043 . 10.1038/367292a0 . 4371932 .
  3. Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D . Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states . Nature . 367 . 6460 . 292–5 . January 1994 . 7510043 . 10.1038/367292a0 . 4371932 .
  4. Degiacomi MT, Iacovache I, Pernot L, Chami M, Kudryashev M, Stahlberg H, van der Goot FG, Dal Peraro M . 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. . Nature Chemical Biology . 9. 6460 . 623–629 . August 2013. 23912165. 10.1038/nchembio.1312 .