TRIM35 mediates protection against influenza infection by activating TRAF3 and degrading viral PB2

查看全文 作　　者：Nan [1]Sun;Li [1]Jiang;Miaomiao [1]Ye;Yihan [1]Wang;Guangwen [1]Wang;Xiaopeng [1]Wan;Yuhui [1]Zhao;Xia [1]Wen;Libin [1]Liang;Shujie [1]Ma;Liling [1]Liu;Zhigao [1]Bu;Hualan [1]Chen;Chengjun [1]Li

机构地区：[1]State Key Laboratory of Veterinary Biotechnology,Harbin Veterinary Research Institute,Chinese Academy of Agricultural Sciences,Harbin 150069,China

出　　处：《Protein & Cell》索引2020年第11卷第12期,共21页

基　　金：The work was supported by the National Key Research and Development Program of China(2016YFD0500205);the National Natural Science Foundation of China(NSFC)(Grant Nos.31521005,31672582,31422054,and 31472215);the Natural Science Foundation of Heilongjiang Province(JQ2019C005);by the Central Public-Interest Scientific Institution Basal Research Fund(No.Y2017JC35). 摘　　要：Tripartite motif(TRIM)family proteins are important effectors of innate immunity against viral infections.Here we identified TRIM35 as a regulator of TRAF3 activation.Deficiency in or inhibition of TRIM35 suppressed the production of type I interferon(IFN)in response to viral infection.777m35-deficient mice were more susceptible to influenza A virus(IAV)infection than were wild-type mice.TRIM35 promoted the RIG-Imediated signaling by catalyzing Lys63-linked polyubiquitination of TRAF3 and the subsequent formation of a signaling complex with VISA and TBK1.IAV PB2 polymerase countered the innate antiviral immune response by impeding the Lys63-linked polyubiquitination and activation of TRAF3.TRIM35 mediated Lys48-linked polyubiquitination and proteasomal degradation of IAV PB2,thereby antagonizing its suppression of TRAF3 activation.Our in vitro and in vivo findings thus reveal novel roles of TRIM35,through catalyzing Lys63-or Lys48-linked polyubiquitination,in RIG-I antiviral immunity and mechanism of defense against IAV infection. 关键词：influenza A virus PB2 TRIM35 TRAF3 UBIQUITINATION antiviral immunity

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TRIM35 mediates protection against influenza infection by activating TRAF3 and degrading viral PB2

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