NTR: perturbation of host inflammasome-mediated signal transduction

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NTR: perturbation of host inflammasome-mediated signal transduction

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@genegodbold please add a few references

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+[Term] +id: GO:0141079 +name: symbiont-mediated activation of host inflammasome-mediated signal transduction +namespace: biological_process +def: "A process in which a symbiont subverts an inflammasome-mediated signal transduction pathway in the host organism by initiating, promoting, or enhancing its activation. The host is defined as the larger of the organisms involved in a symbiotic interaction." [GOC:curators] +is_a: GO:0052029 ! disruption of host signal transduction pathway +property_value: term_tracker_item "https://github.com/geneontology/go-ontology/issues/25685" xsd:anyURI +created_by: pg +creation_date: 2023-07-05T14:20:19Z

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PMID:34155776

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Note to self: reannotate PMID:28331908 and PMID:7689226 with this new term.

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Inflammasome activation by bacteria

• Anthrax lethal factor activates the mouse (but not human) nucleotide-binding domain leucine-rich repeat pyrin domain-containing 1B (NLRP1B) inflammasome by cleaving NLRP1B after Lys44 [PMID:30872531].
• Community-acquired respiratory distress syndrome (CARDS) toxin from Mycoplasma pneumonia activates the host NLRP3 inflammasome by directly ADP-ribosylating it. This leads to subsequent release of interleukin-1beta and associated pathologies [PMID:25538194].
• SpeB fcan cleave inactive human IL-1beta precursor to produce active IL-1beta. The resulting pro-inflammatory cytokine can stimulate nitric oxide synthase activity in vascular smooth muscle cells [PMID:7689226]. Use of IL-1beta inhibitors in mice increases their susceptibility to invasive infections by Group A Streptococcus (GAS) encoding SpeB. SpeB can process IL-1beta during infection to generate a mature inflammatory cytokine that promotes the activity of bactericidal macrophages. Human patients receiving the IL-1beta signaling inhibitor anakinra are 330-fold more likely to experience invasive GAS disease than those not taking the inhibitor and those infections were more lethal and more likely to include necrotizing fasciitis. GAS can induce host inflammation by detection through the NACHT, LRR, and PYD family pyrin domain containing 3 (NLRP3) inflammasome in vitro but NLRP3 is not required for IL-1beta release not for innate immune resistance to the bacterium. IL-1beta is described as an innate immune sensor for microbial proteolysis [PMID:28331908].

Inflammasome suppression by bacteria

• Toll/interleukin-1 receptor (TIR)-domain containing protein (BtpA; Btp1; TcpB) from Brucella abortus interacts with human caspase-4 and promotes ubiquitination (and subsequent destruction) of human caspase-1, caspase-4, and caspase-11. TcpB suppresses caspase-11-mediated secretion of IL-1beta in macrophages infected by brucellae thus attenuating non-canonical inflammasome-mediated pyroptosis and inflammatory responses in both human and mouse macrophages [PMID:29061850].
• Toll/interleukin-1 receptor domain-containing protein (TcpC) from E. coli interacts directly with the NLRP3 inflammasome which is crucial for recognizing pathogens in the host cytosol. IL-1beta release is markedly increased during infection with mutant bacteria lacking TcpC. TcpC attenuates activation of the NLRP3 inflammasome by binding both NLRP3 and caspase-1, preventing the activation of caspase-1 [PMID:27214553].
• Inhibits caspase activation A (IcaA) from Coxiella burnetii inhibits inflammasome activation and subsequent caspase-1 activation in host macrophages by inhibiting host caspase-11-activation of the inflammasome somewhere upstream of caspase-11 [PMID:26687278].
• PtpB is a phosphoinositide phosphatase secreted by Mycobacterium tuberculosis during infection which inhibits host NLRP3 inflammasome-mediated IL-1beta secretion. PtpB dephosphorylates host plasma membrane PI4P and PI(4,5)P2 to inhibit membrane localization of the N-terminal cleavage fragment of gasdermin D which inhibits formation of inflammatory cytokine release and pyroptosis. Activation of phosphoinositide phosphatase activity requires the binding of host ubiquitin by the bacterial enzyme. PtpB inhibits host gasdermin D-dependent cytokine release and subsequent pyroptosis to promote intracellular survival of the bacteria in macrophages [PMID:36227980].
• Protein kinase F (PknF) from Mycobacterium tuberculosis is a serine/threonine kinase involved in suppression of the host NLRP3 inflammasome. A mutant bacterium in which PknF is not expressed induces increased production of IL-1beta through NLRP3, the adaptor protein ASC and caspase-1, when used to infect bone marrow-derived macrophages when compared to wild-type bacteria. In a macrophage model of infection, the mutant bacteria also increased pyroptosis relative to the wild-type bacteria. The working model of the authors is that the absence of PknF decreases activity of the ABC-like transporter protein Rv1747 which results in less secreted phosphatidyl-myo-innositol mannosides (PIMs) that cannot then limit inflammasome activation [PMID:34324582].

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+[Term] +id: GO:0141081 +name: symbiont-mediated suppression of host inflammasome-mediated signal transduction +namespace: biological_process +def: "A process in which a symbiont interferes with, inhibits or stops an inflammasome-mediated signal transduction pathway in the host organism by interfering with its normal execution. The host is defined as the larger of the organisms involved in a symbiotic interaction." [PMID:26687278, PMID:27214553, PMID:29061850, PMID:34324582, PMID:36227980] +synonym: "perturbation of host inflammasome-mediated signal transduction" BROAD [] +is_a: GO:0052028 ! symbiont-mediated activation of host signal transduction pathway +property_value: term_tracker_item "https://github.com/geneontology/go-ontology/issues/25685" xsd:anyURI +created_by: pg +creation_date: 2023-07-10T14:20:22Z