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Viral DNA Binding to NLRC3, an Inhibitory Nucleic Acid Sensor, Unleashes STING, a Cyclic Dinucleotide Receptor that Activates Type I Interferon.

Immunity. 2019; 
Li Xin,Deng Meng,Petrucelli Alex S,Zhu Cheng,Mo Jinyao,Zhang Lu,Tam Jason W,Ariel Pablo,Zhao Baoyu,Zhang Song,Ke Hengming,Li Pingwei,Dokholyan Nikolay V,Duncan Joseph A,Ting Jenny
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Recombinant Proteins … The function of this domain is to bind and hydrolyze ATP, which we and others demonstrated by using purified NLRP3, NLRP12, NOD2, and NLRC4 proteins (Duncan et al., 2007, Hu et al., 2013, Mo et al., 2012 … Mouse Anti-His, GenScript, Cat#A00186-100; RRID: AB_914704 … Get A Quote

摘要

Immune suppression is a crucial component of immunoregulation and a subgroup of nucleotide-binding domain (NBD), leucine-rich repeat (LRR)-containing proteins (NLRs) attenuate innate immunity. How this inhibitory function is controlled is unknown. A key question is whether microbial ligands can regulate this inhibition. NLRC3 is a negative regulator that attenuates type I interferon (IFN-I) response by sequestering and attenuating stimulator of interferon genes (STING) activation. Here, we report that NLRC3 binds viral DNA and other nucleic acids through its LRR domain. DNA binding to NLRC3 increases its ATPase activity, and ATP-binding by NLRC3 diminishes its interaction with STING, thus licensing an I... More

關鍵詞

DNA-binding receptor,NOD-like receptor,STING,TBK1,interf
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