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10.1038/s41392-022-00878-3 http://scihub22266oqcxt.onion/10.1038/s41392-022-00878-3 35075101!8785035!35075101     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=35075101&cmd=llinks): Failed to open stream: HTTP request failed! 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SARS-CoV-2 NSP5 and N protein counteract the RIG-I signaling pathway by suppressing the formation of stress granules |pdf=|usr=}}{{35075101}} gab.com Text SARS-CoV-2 NSP5 and N protein counteract the RIG-I signaling pathway by suppressing the formation of stress granules JO: Signal Transduct Target Ther http://www.kidney.de/pget.php?&tw=1&pmid=35075101 #FOAvip As a highly pathogenic human coronavirus, SARS-CoV-2 has to counteract an intricate network of antiviral host responses to establish infection and spread. The nucleic acid-induced stress response is an essential component of antiviral defense and is closely related to antiviral innate immunity. However, whether SARS-CoV-2 regulates the stress response pathway to achieve immune evasion remains elusive. In this study, SARS-CoV-2 NSP5 and N protein were found to attenuate antiviral stress granule (avSG) formation. Moreover, NSP5 and N suppressed IFN expression induced by infection of Sendai virus or transfection of a synthetic mimic of dsRNA, poly (I:C), inhibiting TBK1 and IRF3 phosphorylation, and restraining the nuclear translocalization of IRF3. Furthermore, HEK293T cells with ectopic expression of NSP5 or N protein were less resistant to vesicular stomatitis virus infection. Mechanistically, NSP5 suppressed avSG formation and disrupted RIG-I-MAVS complex to attenuate the RIG-I-mediated antiviral immunity. In contrast to the multiple targets of NSP5, the N protein specifically targeted cofactors upstream of RIG-I. The N protein interacted with G3BP1 to prevent avSG formation and to keep the cofactors G3BP1 and PACT from activating RIG-I. Additionally, the N protein also affected the recognition of dsRNA by RIG-I. This study revealed the intimate correlation between SARS-CoV-2, the stress response, and innate antiviral immunity, shedding light on the pathogenic mechanism of COVID-19. Twit Text FOAVip SARS-CoV-2 NSP5 and N protein counteract the RIG-I signaling pathway by suppressing the formation of stress granules ????Signal Transduct Target Ther http://www.kidney.de/pget.php?&tw=1&pmid=35075101 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35075101 #FOAvip English Wikipedia <ref>{{Cite pmid|35075101}}</ref> SARS-CoV-2 NSP5 and N protein counteract the RIG-I signaling pathway by suppressing the formation of stress granules #MMPMID35075101 Zheng Y; Deng J; Han L; Zhuang MW; Xu Y; Zhang J; Nan ML; Xiao Y; Zhan P; Liu X; Gao C; Wang PH Signal Transduct Target Ther 2022[Jan]; 7 (1): 22 PMID35075101show ga As a highly pathogenic human coronavirus, SARS-CoV-2 has to counteract an intricate network of antiviral host responses to establish infection and spread. The nucleic acid-induced stress response is an essential component of antiviral defense and is closely related to antiviral innate immunity. However, whether SARS-CoV-2 regulates the stress response pathway to achieve immune evasion remains elusive. In this study, SARS-CoV-2 NSP5 and N protein were found to attenuate antiviral stress granule (avSG) formation. Moreover, NSP5 and N suppressed IFN expression induced by infection of Sendai virus or transfection of a synthetic mimic of dsRNA, poly (I:C), inhibiting TBK1 and IRF3 phosphorylation, and restraining the nuclear translocalization of IRF3. Furthermore, HEK293T cells with ectopic expression of NSP5 or N protein were less resistant to vesicular stomatitis virus infection. Mechanistically, NSP5 suppressed avSG formation and disrupted RIG-I-MAVS complex to attenuate the RIG-I-mediated antiviral immunity. In contrast to the multiple targets of NSP5, the N protein specifically targeted cofactors upstream of RIG-I. The N protein interacted with G3BP1 to prevent avSG formation and to keep the cofactors G3BP1 and PACT from activating RIG-I. Additionally, the N protein also affected the recognition of dsRNA by RIG-I. This study revealed the intimate correlation between SARS-CoV-2, the stress response, and innate antiviral immunity, shedding light on the pathogenic mechanism of COVID-19. |Animals[MESH] |Chlorocebus aethiops[MESH] |Coronavirus 3C Proteases/*genetics/immunology[MESH] |Coronavirus Nucleocapsid Proteins/*genetics/immunology[MESH] |DEAD Box Protein 58/*genetics/immunology[MESH] |DNA Helicases/*genetics/immunology[MESH] |Gene Expression Regulation[MESH] |HEK293 Cells[MESH] |HeLa Cells[MESH] |Humans[MESH] |Immune Evasion[MESH] |Phosphoproteins/genetics/immunology[MESH] |Poly I-C/pharmacology[MESH] |Poly-ADP-Ribose Binding Proteins/*genetics/immunology[MESH] |Protein Binding[MESH] |RNA Helicases/*genetics/immunology[MESH] |RNA Recognition Motif Proteins/*genetics/immunology[MESH] |RNA, Double-Stranded/genetics/immunology[MESH] |RNA-Binding Proteins/*genetics/immunology[MESH] |Receptors, Immunologic/*genetics/immunology[MESH] |SARS-CoV-2/*genetics/immunology/pathogenicity[MESH] |Sendai virus/genetics/immunology[MESH] |Signal Transduction[MESH] |Stress Granules/drug effects/*genetics/immunology/virology[MESH] |Vero Cells[MESH]SARS-CoV-2 NSP5 and N protein counteract the RIG-I signaling pathway b(epmc).pdf DeepDyve Pubget Overpricing