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Details on Person Shigella flexneri, a Gram-negative bacterium that damages th...
| Class:Id | Summation:9956645 |
|---|---|
| _displayName | Shigella flexneri, a Gram-negative bacterium that damages th... |
| _timestamp | 2025-08-14 15:54:24 |
| created | [InstanceEdit:9956599] Shamovsky, Veronica, 2025-06-13 |
| literatureReference | [LiteratureReference:9956643] Shigella evades pyroptosis by arginine ADP-riboxanation of caspase-11 [LiteratureReference:9956675] The Shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory cell death, and promotes epithelial infection [LiteratureReference:9956594] Structural mechanisms of calmodulin activation of Shigella effector OspC3 to ADP-riboxanate caspase-4/11 and block pyroptosis |
| modified | [InstanceEdit:9958687] Shamovsky, Veronica, 2025-06-24 [InstanceEdit:9960531] Shamovsky, Veronica, 2025-07-14 [InstanceEdit:9963557] Shamovsky, Veronica, 2025-08-14 [InstanceEdit:9963583] Shamovsky, Veronica, 2025-08-14 |
| text | Shigella flexneri, a Gram-negative bacterium that damages the colonic epithelium and causes bacillary dysentery in humans, secretes the effector OspC3 via the type III secretion system. OspC3 inhibits caspase-4 (CASP4) and suppresses CASP4-mediated pyroptosis, a lytic form of cell death triggered by intracellular lipopolysaccharide (LPS) (Kobayashi T. et al., 2013; Li Z. et al., 2021; Hou Y. et al., 2023). Structural and biochemical analyses have shown that OspC3 recognizes CASP4 via its ankyrin repeat domain (Kobayashi T. et al., 2013; Li Z. et al., 2021; Hou Y. et al., 2023). OspC3 can bind both procaspase (p30) and processed (p20:p10; not depicted in this Reactome event) forms of CASP4 (Li Z. et al., 2021). It catalyzes ADP-riboxanation of CASP4 at arginine 314 (R314) by transferring ADP-ribose from NAD⁺ to the Nδ atom of the arginine side chain, followed by deamination of an Nω group to generate an oxazolidine ring structure (Li Z. et al., 2021; Hou Y. et al., 2023). The catalytic activity of OspC3 is enhanced by calcium-free calmodulin (CALM), which binds OspC3 and reconfigures its catalytic pocket to permit NAD⁺ binding. CALM binding also promotes the formation of a stable ternary complex between CALM:OspC3 and CASP4 (Li Z. et al., 2021; Hou Y. et al., 2023). |
| (summation) | [Reaction:9956667] CASP4 binds CALM:OspC3 [Homo sapiens] |
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No pathways have been reviewed or authored by Shigella flexneri, a Gram-negative bacterium that damages th... (9956645)
