The Open Toxinology Journal · 2010 · 51 citations · 97 references
Life SciencesMicrobiologyMicrobial GeneticsMicrobial SystematicsStructural BiologyBacterial PathogenesisBacterial ToxinsToxin ProductionBacterial Toxin BiologyPathogenesis Of Bacterial ToxinsPore-forming ToxinsProtein ToxinsToxin AssemblyToxin FunctionToxin Structure
Pore-forming toxins (PFTs) represent the largest known group of bacterial protein toxins to date.Membrane insertion and subsequent pore-formation occurs after initial binding to cell-surface receptor and oligomerization.Aerolysin, a toxin produced by the Gram-negative bacterium Aeromonas hydrophila and related species, belongs to the PFT group and shares a common mechanism of action involving -barrel structures resulting from the assembly ofhairpins from individual toxin monomers into a heptamer.Aerolysin is also the name given to structurally and mechanistically related toxins called the aerolysin-like toxin family.A universal characteristic of this toxin family involves the diverse life forms that synthesize these proteins throughout Nature.Examples include: 1) epsilon-toxin and septicum-alpha-toxin produced by anaerobic, Gram-positive Clostridium species; 2) enterolobin by the Brazilian tree Enterolobium contortisiliquum; 3) a mushroom toxin Laetiporus sulphureus lectin (LSL); 4) mosquitocidal toxins (Mtxs) from the Gram-positive bacteria Bacillus sphaericus and parasporine-2 from Bacillus thuringiensis; and 6) hydralysins from the tiny aquatic animal Chlorohydra viridis.The following review provides an overview of the different members within the aerolysin-like toxin family.
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What should be called a lectin?
Irwin Goldstein, R. Colin Hughes, Michel Monsigny et al. · Nature · 1980 · 880 citations · Full text
Crystal structure of the anthrax toxin protective antigen
Carlo Petosa, R. John Collier, Kurt R. Klimpel et al. · Nature · 1997 · 755 citations
Life Sciences, Biochemistry, Biology +14