分子免疫学固有免疫gaobo40925.ppt

（1）RIG-1和MDA-5是胞质溶胶中识别病毒双链RNA的感知元件。（3)而且RLR本身是干扰素诱导蛋白。基本结构N端为效应结构域CARD，C端为RNA解旋酶结构域，与之发生作用的衔接蛋白IPS1同型互作，分别通过核因子和干扰素调节因子激活促炎症细胞因子和I型干扰素Recognition of microbial RNA and DNA by cytoplasmic pattern recognition receptors. RIG-I and MDA5 recognize 5’-triphosphate ssRNA and dsRNA from RNA viruses and trigger signaling cascades via a CARD-containing adaptor molecule, IPS-1. IPS-1 induces the expression of genes for type I interferons and pro-inflammatory cytokines by activating transcription factors of the IRF and NFκB families. The role of LGP2 in RNA virus recognition is unclear and LGP2 has been proposed to inhibit RIG-I activity. DAI recognizes dsDNA and induces gene expression through an unknown adaptor molecule. Modular structures of the receptor proteins are shown with the abbreviations of the domains as follows: CARD, caspase activating recruitment domains; helicase, RNA-binding domain; RD, repressor domain; TM, transmembrane domain; Zα and Zβ, Z-DNA binding domain α and β; D3, tentative name for an additional DNA-binding region; SD, signaling domain. IFI16 (IFN-γ-inducible protein 16) is related to the DNA sensor AIM2 * * * * DAI was firstly implicated as a cytoplasmic DNA sensor, but studies with DAI-deficient mice suggest that its function is redundant IFI16 (IFN-γ-inducible protein 16) is related to the DNA sensor AIM2. IFI16 has been reported to induce ASC-dependent inflammasome activation during infection with nuclear DNA viruses and has a second unexpected func-tion as an inducer of IFN-  in response intracellular DNA Helicase DDX41 hasbeen proposed to act ‘upstream’ of STING, by binding to cyclicdi-nucleotides, and then promoting the binding of STING to these molecules resulting in STING activation The catalytic subunit of DNA-dependentprotein kinase (DNA-PKcs), its binding partners Ku70/80 and the kinase ATM were shown to be dispensable for the IFN response to intracellular DNA in murinebone marrow-derived macrophages Recently, Mre11 (Meiotic recombin