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Details on Person SARS-CoV-1 nsp1 induces a near-complete shutdown of host pro...
| Class:Id | Summation:9729821 |
|---|---|
| _displayName | SARS-CoV-1 nsp1 induces a near-complete shutdown of host pro... |
| _timestamp | 2023-01-24 21:38:40 |
| created | [InstanceEdit:9729799] Stephan, Ralf, 2021-05-03 |
| modified | [InstanceEdit:9755974] Shamovsky, Veronica, 2021-10-12 [InstanceEdit:9762469] Stephan, Ralf, 2022-01-25 [InstanceEdit:9825270] Shamovsky, Veronica, 2023-01-24 |
| text | SARS-CoV-1 nsp1 induces a near-complete shutdown of host protein translation by both binding to ribosome subunits, blocking canonical mRNA translation, and by endonucleolytic cleavage and subsequent degradation of host mRNAs (Kamitani et al, 2009). SARS-CoV-2 nsp1 protein binds to the 18S rRNA subunit of the 40S ribosomal complex, which is both part of the 43S pre-initiation complex and the 80S ribosome. Nsp1 binds in the mRNA entrance channel on the 40S subunit, where it would partially overlap with the fully accommodated mRNA. The nsp1 C-terminal domain is necessary and sufficient for translation inhibition. By this mechanism, nsp1 substantially downregulates the innate immune responses (Burke et al, 2021; Slavin et al, 2021; Banerjee et al, 2020; Schubert et al, 2020; Thoms et al, 2020; Yuan et al, 2020; Lapointe et al, 2021). It appears that translation inhibition is not universal. Functionally related genes, including components of the translation and folding machinery, preferentially escape Nsp1-dependent translation inhibition. Highly translated genes overwhelmingly have 5′ terminal oligopyrimidine (TOP) motifs, suggesting a mechanism for their selective translational response (Rao et al, 2020). In addition to widespread shutdown of host protein translation, cis-acting RNA hairpin SL1 in the leader sequence of SARS-CoV-2 RNA facilitates evasion of viral RNAs from the nsp1-induced translational suppression (Banerjee et al, 2020; Schubert et al, 2020; Shi et al, 2020; Tidu et al, 2021). Further, the N-terminal domain of nsp1 promotes 40S-mediated viral, but not host, mRNA recognition and translation (Mendez et al, 2021; Wang et al, 2023) |
| (summation) | [Reaction:9729849] SARS-CoV-2 nsp1 binds to 40S ribosomal complex [Homo sapiens] |
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No pathways have been reviewed or authored by SARS-CoV-1 nsp1 induces a near-complete shutdown of host pro... (9729821)
