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| α-Hemolysin/HlyA |
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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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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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CyaA/ACT
(Invasive Adenylate cyclase /haemolysin) |
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Originally identified as a hemolysin because it will lyse red blood cells. Secreted by type I pathway and secretion requires CyaB, D, E proteins. ... |
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| RtxA |
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Secreted through an LssB-LssD-TolC type I secretion system. The N-terminal, involved in adhesion, and the C-terminal region, involved in adhesion and pore formation in the host membranes. Two other types of domains were commonly identified in all the rtx genes: the VWA domain involved in adhesion processes, and another tandem repeated domain related to cytotoxic activity, the haemolysin calcium-binding (HemolysinCabind) site. ... |
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| δ-hemolysin |
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Capable of lysing erythrocytes and other mammalian cells, as well as subcellular structures. Forms α-helix with hydrophobic and hydrophilic domains on opposite sides and aggregates to form channels channels in the membrane. ... |
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| CAMP factor |
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CAMP factor, a pore-forming protein toxin of ~24 kDa gives rise to the so-called CAMP reaction, which consists of a zone of strong hemolysis that is observed when S. agalactiae is streaked next to Staphylococcus aureus on sheep blood agar. S. aureus secretes sphingomyelinase. Sheep red blood cells are rich in sphingomyelin and, upon exposure to sphingomyelinase, become greatly sensitized to CAMP factor, which then effects hemolysis. This co-hemolytic phenomenon was first described by Christie, Atkins, and Munch-Petersen, and the “CAMP” acronym represents these investigators' last names. Paralogs of CAMP factor genes have been sequenced in a wide range of Gram-positive pathogens, including Streptococcus uberisand Cutibacterium acnes. ... |
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| PirAB |
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Marine bacterial binary toxin PirA and PirB encoded in the pVA1 plasmid. The assembled PirA and PirB structure is similar to Bacillus thuringiensis Cry toxins: the N-terminal and C-terminal of PirB correspond to the pore-forming domain I and the receptor-binding domain II of Cry protein, respectively, while PirA corresponds to Cry toxin domain III, which is the sugar-binding domain. ... |
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| YaxAB |
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Both YaxA and YaxB are required for cytotoxic activity. Structural homology of YaxA are pore-forming toxins HblB (from Bacillus cereus) and HlyE (from E. coli). YaxA PDB code: 6EK7. YaxB PDB code: 6EK8. ... |
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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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