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10.1126/science.abc8665 http://scihub22266oqcxt.onion/10.1126/science.abc8665 32680882!7402621!32680882     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32680882&cmd=llinks): Failed to open stream: HTTP request failed! 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Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2 |pdf=|usr=}}{{32680882}} gab.com Text Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2 JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32680882 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the current coronavirus disease 2019 (COVID-19) pandemic. A major virulence factor of SARS-CoVs is the nonstructural protein 1 (Nsp1), which suppresses host gene expression by ribosome association. Here, we show that Nsp1 from SARS-CoV-2 binds to the 40S ribosomal subunit, resulting in shutdown of messenger RNA (mRNA) translation both in vitro and in cells. Structural analysis by cryo-electron microscopy of in vitro-reconstituted Nsp1-40S and various native Nsp1-40S and -80S complexes revealed that the Nsp1 C terminus binds to and obstructs the mRNA entry tunnel. Thereby, Nsp1 effectively blocks retinoic acid-inducible gene I-dependent innate immune responses that would otherwise facilitate clearance of the infection. Thus, the structural characterization of the inhibitory mechanism of Nsp1 may aid structure-based drug design against SARS-CoV-2. Twit Text FOAVip Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2 ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32680882 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32680882 #FOAvip English Wikipedia <ref>{{Cite pmid|32680882}}</ref> Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2 #MMPMID32680882 Thoms M; Buschauer R; Ameismeier M; Koepke L; Denk T; Hirschenberger M; Kratzat H; Hayn M; Mackens-Kiani T; Cheng J; Straub JH; Sturzel CM; Frohlich T; Berninghausen O; Becker T; Kirchhoff F; Sparrer KMJ; Beckmann R Science 2020[Sep]; 369 (6508): 1249-1255 PMID32680882show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the current coronavirus disease 2019 (COVID-19) pandemic. A major virulence factor of SARS-CoVs is the nonstructural protein 1 (Nsp1), which suppresses host gene expression by ribosome association. Here, we show that Nsp1 from SARS-CoV-2 binds to the 40S ribosomal subunit, resulting in shutdown of messenger RNA (mRNA) translation both in vitro and in cells. Structural analysis by cryo-electron microscopy of in vitro-reconstituted Nsp1-40S and various native Nsp1-40S and -80S complexes revealed that the Nsp1 C terminus binds to and obstructs the mRNA entry tunnel. Thereby, Nsp1 effectively blocks retinoic acid-inducible gene I-dependent innate immune responses that would otherwise facilitate clearance of the infection. Thus, the structural characterization of the inhibitory mechanism of Nsp1 may aid structure-based drug design against SARS-CoV-2. |*Immune Evasion[MESH] |*Immunity, Innate[MESH] |*Protein Biosynthesis[MESH] |Betacoronavirus/*chemistry/immunology/metabolism/physiology[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Coronavirus Infections/immunology/virology[MESH] |Cryoelectron Microscopy[MESH] |DEAD Box Protein 58/genetics/metabolism[MESH] |Humans[MESH] |Interferon-beta/genetics/metabolism[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Pneumonia, Viral/immunology/virology[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Interaction Domains and Motifs[MESH] |Protein Structure, Secondary[MESH] |RNA, Messenger/metabolism[MESH] |Receptors, Immunologic[MESH] |Ribosome Subunits, Small, Eukaryotic/chemistry/metabolism[MESH] |SARS-CoV-2[MESH]Structural basis for translational shutdown and immune evasion by the (epmc).pdf DeepDyve Pubget Overpricing