Abstract
Many pathogenic bacteria produce toxins that act as pore-forming toxins (PFTs) on the cytoplasmic membrane of eukaryotic target cells. Precursors of PFTs are water-soluble and undergo major conformation changes upon binding to receptors or to lipids on the cell surface. Major structural features of PFTs are alpha-helices or beta strands forming cylinders with a hydrophilic interior and a hydrophobic exterior. This chapter deals with structural aspects of PFTs that form alpha-helical structures such as ClyA (Escherichia coli Hemolysin E, HlyE, SheA) of enteric bacteria, the insecticidal pore-forming toxins of the Cry family produced by different Bacillus thuringiensis strains and by the tripartite ABC-type toxin complex of Photorhabdus luminescens and related Tc-toxin complexes. Similarly, structural properties of toxins are discussed that form beta-barrel cylinders in biological and artificial membranes. These toxins are alpha-hemolysin of Staphilococcus aureus, epsilon-toxin, aerolysin and related toxins and the binding component channels of binary A-B type of toxins. In all these cases the PFTs form oligomeric structures (hexamers, heptamers and octamers) where one monomer contributes two beta-strands to the pore-forming complex.
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