Aerolysin

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Aerolysin
PDB 1pre EBI.jpg
proaerolysin
Identifiers
Symbol Aerolysin
Pfam PF01117
Pfam clan CL0345
InterPro IPR005830
PROSITE PDOC00247
SCOP 1pre
SUPERFAMILY 1pre
TCDB 1.C.4
OPM superfamily 35

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] 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] Images of an aerolysin oligomer derived from electron microscopy and molecular dynamics simulations 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.[3]

References[edit]

  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. PMC 212202. PMID 3584074. 
  2. ^ a b 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. 
  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.". Nature Chemical Biology 9 (6460): 623–629. doi:10.1038/nchembio.1312. PMID 23912165. 

This article incorporates text from the public domain Pfam and InterPro IPR005830