Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2.
Betacoronavirus
/ chemistry
Binding Sites
COVID-19
Coronavirus Infections
/ immunology
Cryoelectron Microscopy
DEAD Box Protein 58
/ genetics
Humans
Immune Evasion
Immunity, Innate
Interferon-beta
/ genetics
Models, Molecular
Pandemics
Pneumonia, Viral
/ immunology
Protein Binding
Protein Biosynthesis
Protein Domains
Protein Interaction Domains and Motifs
Protein Structure, Secondary
RNA, Messenger
/ metabolism
Receptors, Immunologic
Ribosome Subunits, Small, Eukaryotic
/ chemistry
SARS-CoV-2
Viral Nonstructural Proteins
/ chemistry
Journal
Science (New York, N.Y.)
ISSN: 1095-9203
Titre abrégé: Science
Pays: United States
ID NLM: 0404511
Informations de publication
Date de publication:
04 09 2020
04 09 2020
Historique:
received:
18
05
2020
accepted:
13
07
2020
pubmed:
19
7
2020
medline:
20
9
2020
entrez:
19
7
2020
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 32680882
pii: science.abc8665
doi: 10.1126/science.abc8665
pmc: PMC7402621
doi:
Substances chimiques
NSP1 protein, SARS-CoV-2
0
RNA, Messenger
0
Receptors, Immunologic
0
Viral Nonstructural Proteins
0
Interferon-beta
77238-31-4
RIGI protein, human
EC 3.6.1.-
DEAD Box Protein 58
EC 3.6.4.13
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1249-1255Commentaires et corrections
Type : CommentIn
Informations de copyright
Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
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