PMC:7200337 / 9095-10644 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7200337","sourcedb":"PMC","sourceid":"7200337","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7200337","text":"Following activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. Although no experimental studies have delineated the precise functions of SARS-CoV-2 proteins, proteomic studies have demonstrated interactions between viral proteins and PRR signaling cascades. SARS-CoV-2 ORF9b indirectly interacts with the signaling adaptor MAVS via its association with Tom70 (Gordon et al., 2020), consistent with prior reports that SARS-CoV-1 ORF9b suppresses MAVS signaling (Shi et al., 2014). Furthermore, SARS-CoV-2 NSP13 interacts with signaling intermediate TBK1, and NSP15 is associated with RNF41, an activator of TBK1 and IRF3 (Gordon et al., 2020). Similarly, SARS-CoV-1 M protein is known to inhibit the TBK1 signaling complex (Siu et al., 2009), as does MERS-CoV ORF4b (Yang et al., 2015). Other proteins, including SARS-CoV-1 PLP, N, ORF3b, and ORF6, block IRF3 phosphorylation and nuclear translocation (Devaraj et al., 2007, Kopecky-Bromberg et al., 2007). NF-kB is also inhibited by CoV proteins. These include SARS-CoV-1 PLP (Frieman et al., 2009) and MERS-CoV ORF4b and ORF5 (Canton et al., 2018, Menachery et al., 2017). Finally, SARS-CoV-1 NSP1 (Huang et al., 2011a, Kamitani et al., 2009) and MERS-CoV NSP1 (Lokugamage et al., 2015) initiate general inhibition of host transcription and translation, thus limiting antiviral defenses 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