I(nsp1)ecting SARS-CoV-2-ribosome interactions.

Details

Ressource 1Download: simeoni_2021-final version.pdf (141.84 [Ko])
State: Public
Version: Author's accepted manuscript
License: CC BY 4.0
Serval ID
serval:BIB_AE1D3DB18448
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Institution
Title
I(nsp1)ecting SARS-CoV-2-ribosome interactions.
Journal
Communications biology
Author(s)
Simeoni M., Cavinato T., Rodriguez D., Gatfield D.
ISSN
2399-3642 (Electronic)
ISSN-L
2399-3642
Publication state
Published
Issued date
10/06/2021
Peer-reviewed
Oui
Volume
4
Number
1
Pages
715
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Review
Publication Status: epublish
Abstract
While SARS-CoV-2 is causing modern human history's most serious health crisis and upending our way of life, clinical and basic research on the virus is advancing rapidly, leading to fascinating discoveries. Two studies have revealed how the viral virulence factor, nonstructural protein 1 (Nsp1), binds human ribosomes to inhibit host cell translation. Here, we examine the main conclusions on the molecular activity of Nsp1 and its role in suppressing innate immune responses. We discuss different scenarios potentially explaining how the viral RNA can bypass its own translation blockage and speculate on the suitability of Nsp1 as a therapeutic target.
Keywords
5' Untranslated Regions, Gene Expression Regulation, Viral, Host-Pathogen Interactions/physiology, Humans, Immunity, Innate, Protein Biosynthesis, RNA, Messenger/metabolism, Ribosomes/metabolism, Ribosomes/virology, SARS-CoV-2/genetics, SARS-CoV-2/pathogenicity, Viral Nonstructural Proteins/chemistry, Viral Nonstructural Proteins/genetics, Viral Nonstructural Proteins/metabolism
Pubmed
Web of science
Open Access
Yes
Create date
29/06/2021 10:41
Last modification date
03/07/2021 5:32
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