6zme
From Proteopedia
Jump to navigationJump to search
SARS-CoV-2 Nsp1 bound to the human CCDC124-80S-eERF1 ribosome complex
| ||||||||||||
Structural highlights
FunctionPublication Abstract from PubMedSARS-CoV-2 is the causative agent of the current 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 mRNA translation both in vitro and in cells. Structural analysis by cryo-electron microscopy (cryo-EM) 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 RIG-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. Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2.,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 Jul 17. pii: science.abc8665. doi: 10.1126/science.abc8665. PMID:32680882[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
| ||||||||||||||||||||
This page was last modified 18:51, 8 September 2026.