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| Cytolysin |
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Production and activation of cytolysin involves the products of a complex operon of eight genes and that this operon can be located on either pheromone-responsive plasmids or on the chromosome within a pathogenicity island. Most of this gene locus is absent in E. faecalis V583 due to a 17-kbp deletion. Cytolysin expression is regulated by one of the subunits (CylLS'') through a quorum-sensing autoinduction mechanism. ... |
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| α-Hemolysin |
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Best-characterized RTX protein secreted by a type I secretion system: the structural gene encoding the hemolysin (hlyA) is part of an operon that also encodes a dedicated export system (HlyB and HlyD comprising a type I secretion system) and a toxin modifying enzyme (HlyC). The HlyC protein is responsible for acylation of HlyA, resulting in toxin activation. The hly operon is found on a plasmid of EHEC O157:H7, while the hly operon is often located adjacent to the P fimbrial genes on the same pathogenicity island on the chromosome of UPEC strains. ... |
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LLS
(Listeriolysin S) |
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Haemolysin LLS is post-translationally modified and belongs to a family of modified virulence peptides, including streptolysin S and several as-yet uncharacterized members of the same family in other pathogens. ... |
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| Aerolysin |
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PDB code: 1PRE. Aerolysin is produced as an inactive precursor, proaerolysin, which contains a C-terminal peptide (CTP) required for folding into its soluble form. Proteolysis in the loop that connects the CTP to the main body allows aerolysin to oligomerize in a heptameric ring-like complex that inserts into the target membrane to form the pore. Proaerolysin is an L-shaped molecule. Domain 1, involved in binding N-linked oligosaccharides. Domain 2, involved in binding the glycan core of the glycosyl phosphatidylinositol (GPI)-anchored aerolysin receptors. Domain 3, involved in oligomerization. Domain 4, contains the CTP. ... |
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ALO
(Anthrolysin O) |
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Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
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CytK
(Cytotoxin K, Haemolysin IV) |
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Belongs to the family of oligomeric β-barrel pore-forming toxins. Haemolytic and cytotoxic activity. ... |
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HBL
(Haemolysin BL) |
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This enterotoxin is toxic only as a ternary complex. Neither any binary combination of the components nor any individual component is toxic in its own right. ... |
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Nhe
(Nonhemolytic enterotoxin) |
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The respective HBL and NHE proteins share 23~40% sequence identity. Tripartite pore-forming toxin that require the combined action of the three proteins a cytolytic protein NheA, and two binding components NheB and NheC. All three proteins are required for maximum biological activity. ... |
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| alpha-toxin (septicum) |
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Secreted via type II secretion pathway. Secreted as inactive protoxin monomers that bind to GPI-anchored proteins on the target cell. The bound monomers are then cleaved and activated by host cell proteases, allowing them to oligomerize into a heptameric complex and insert to form a 1.6 nm β-barrel pore. ... |
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| beta-toxin (CPB) |
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Beta-toxin is released by C. perfringens types B and C, and is the main lethal factor in type C strains. The protein has a molecular mass of 34 kDa and is highly trypsin-sensitive. ... |
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