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• W2955145078 abstract "Inflammasomes are cytosolic multi-protein complexes that detect infection or cellular damage and activate the Caspase-1 (CASP1) protease. The NAIP5/NLRC4 inflammasome detects bacterial flagellin and is essential for resistance to the flagellated intracellular bacterium Legionella pneumophila. The effectors required downstream of NAIP5/NLRC4 to restrict bacterial replication remain unclear. Upon NAIP5/NLRC4 activation, CASP1 cleaves and activates the pore-forming protein Gasdermin-D (GSDMD) and the effector caspase-7 (CASP7). However, Casp1–/– (and Casp1/11–/–) mice are only partially susceptible to L. pneumophila and do not phenocopy Nlrc4–/–mice, because NAIP5/NLRC4 also activates CASP8 for restriction of L. pneumophila infection. Here we show that CASP8 promotes the activation of CASP7 and that Casp7/1/11–/– and Casp8/1/11–/– mice recapitulate the full susceptibility of Nlrc4–/– mice. Gsdmd–/– mice exhibit only mild susceptibility to L. pneumophila, but Gsdmd–/–Casp7–/– mice are as susceptible as the Nlrc4–/– mice. These results demonstrate that GSDMD and CASP7 are the key substrates downstream of NAIP5/NLRC4/CASP1/8 required for resistance to L. pneumophila." @default.
• W2955145078 created "2019-07-12" @default.
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• W2955145078 date "2019-06-28" @default.
• W2955145078 modified "2023-10-01" @default.
• W2955145078 title "Gasdermin-D and Caspase-7 are the key Caspase-1/8 substrates downstream of the NAIP5/NLRC4 inflammasome required for restriction of Legionella pneumophila" @default.
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• W2955145078 doi "https://doi.org/10.1371/journal.ppat.1007886" @default.
• W2955145078 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6622555" @default.
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