|Title||Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2.|
|Journal, issue, pages||Science, Vol. 369, Issue 6508, Page 1249-1255, Year 2020|
|Publish date||Sep 4, 2020|
|Authors||Matthias Thoms / Robert Buschauer / Michael Ameismeier / Lennart Koepke / Timo Denk / Maximilian Hirschenberger / Hanna Kratzat / Manuel Hayn / Timur Mackens-Kiani / Jingdong Cheng / Jan H Straub / Christina M Stürzel / Thomas Fröhlich / Otto Berninghausen / Thomas Becker / Frank Kirchhoff / Konstantin M J Sparrer / Roland Beckmann /|
|PubMed Abstract||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 ...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 40 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 Nsp1-40 and various native Nsp1-40 and -80 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.|
|External links||PubMed:32680882 / Publisher's page|
|Keywords||Betacoronavirus / Binding Sites / Coronavirus Infections / Cryoelectron Microscopy / DDX58 protein, human / DEAD Box Protein 58 / Humans / Immune Evasion / Immunity, Innate / Interferon-beta / Models, Molecular / NSP1 protein, SARS-CoV-2 / Pandemics / Pneumonia, Viral / Protein Binding / Protein Biosynthesis / Protein Domains / Protein Interaction Domains and Motifs / Protein Structure, Secondary / RNA, Messenger / Ribosome Subunits, Small, Eukaryotic / Viral Nonstructural Proteins / VIRAL PROTEIN / Translational Inhibition / SARS-CoV-2 / Human Ribosome|
|Methods||EM (single particle)|
|Resolution||2.6 - 3.2 A|
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