About: A novel two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	A novel two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein
Creator	Makino, Shinji Huang, Cheng Narayanan, Krishna Kamitani, Wataru Lokugamage, Kumari
source	Medline; PMC
abstract	Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression, including type I interferon production, by promoting host mRNA degradation and inhibiting host translation, in infected cells. We present evidence that nsp1 uses a novel, two-pronged strategy to inhibit host translation/gene expression. Nsp1 bound to the 40S ribosomal subunit and inactivated the translational activity of the 40S subunits. Furthermore, the nsp1-40S ribosome complex induced the modification of the 5'-region of capped mRNA template and rendered the template RNA translationally incompetent. Nsp1 also induced RNA cleavage in templates carrying the internal ribosome entry site (IRES) from encephalomyocarditis virus, but not in those carrying IRESs from hepatitis C and cricket paralysis viruses, demonstrating that the nsp1-induced RNA modification was template-dependent. We speculate that the mRNAs that underwent the nsp1-mediated modification are marked for rapid turnover by the host RNA degradation machinery.
has issue date	2009-10-18(xsd:dateTime)
bibo:doi	10.1038/nsmb.1680
bibo:pmid	19838190
has license	no-cc
sha1sum (hex)	a8834bb33602430375ca8176a8e3176cf8e0e085
schema:url	https://doi.org/10.1038/nsmb.1680
resource representing a document's title	A novel two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein
has PubMed Central identifier	PMC2784181
has PubMed identifier	19838190
schema:publication	Nat Struct Mol Biol
resource representing a document's body	covid:a8834bb33602430375ca8176a8e3176cf8e0e085#body_text
is schema:about of	named entity 'mRNA degradation' named entity 'RNA' named entity 'viruses' named entity 'mRNA template' named entity 'RNA modification' named entity 'type I interferon' named entity '40S ribosome' named entity 'cricket' named entity 'RNA' named entity '40S' named entity 'RNA' named entity 'RNA' named entity '48S' named entity 'RNA' named entity '40S' named entity 'CrPV IRES' named entity 'IRES' named entity 'RNA' named entity '80S' named entity 'GST' named entity 'Western blot' named entity 'mRNA degradation' named entity 'N-terminal' named entity 'phosphate group' named entity 'complex formation' named entity 'RNA' named entity 'RNA' named entity '40S' named entity 'RNA' named entity 'ribosomes' named entity 'GMP' named entity '48S' named entity 'centrifugation' named entity 'GST' named entity 'mouse hepatitis virus' named entity 'RNA' named entity 'ribosomal subunit' named entity 'untranslated region' named entity 'mRNAs' named entity 'mRNAs' named entity '5′-end' named entity 'IRES' named entity 'gene' named entity 'ribosomal subunits' named entity 'myc' named entity 'RNA' named entity 'RNA' named entity 'primer extension' named entity 'mRNA degradation' named entity 'EMCV' named entity 'RNA' named entity 'GST' named entity 'ribosomes' named entity 'RNA' named entity '3′-end' named entity 'RNA' named entity 'cap-dependent' named entity 'molecular level' named entity 'chloramphenicol acetyltransferase' named entity 'RNA' named entity 'Severe acute respiratory syndrome' named entity 'cleavage' named entity 'RNA' named entity 'RNA' named entity 'causative agent' named entity 'SARS' named entity '48S' named entity 'Primer extension' named entity 'supernatant' named entity 'immunoprecipitated' named entity 'sequencing gel' named entity 'ribosomes' named entity 'RNA' named entity 'RNA modification' named entity 'RNA' named entity 'RNA' named entity 'gene translation'

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