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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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SSLs
(Staphylococcal superantigen-like proteins) |
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A family of 14 proteins located on two genomic clusters. Share structural similarities with superantigens, but unlike superantigens, the SSL proteins do not bind MHC receptor or T cell receptors to elicit a toxic cytokine response. ... |
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| β-haemolysin/cytolysin |
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Lyses not only red blood cells but a broad range of eukaryotic cell types. Surface associated protein that can be extracted from the cells by non-ionic detergent, starch or albumin. ... |
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| Phospholipase C |
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Contribute to the pathogenesis by aiding in the lysis of host cells, via cleavage of phospholipids present in the host cell membrane, and by degrading phospholipids present at mucosal barriers to facilitate bacterial invasion. ... |
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| Phospholipase D |
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Contribute to the pathogenesis by aiding in the lysis of host cells, via cleavage of phospholipids present in the host cell membrane, and by degrading phospholipids present at mucosal barriers to facilitate bacterial invasion. ... |
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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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