About: The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/MDA5 activation

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/MDA5 activation Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/MDA5 activation
Creator	Fang, Liurong Wang, Dang Xiao, Shaobo Ding, Zhen Zhao, Ling Wang, Xunlei Long, Siwen Wang, Mohan Yuan, Shuangling Foda, Mohamed
Source	Medline; PMC
abstract	Coronaviruses (CoVs) are a huge threat to both humans and animals and have evolved elaborate mechanisms to antagonize interferons (IFNs). Nucleocapsid (N) protein is the most abundant viral protein in CoV-infected cells, and has been identified as an innate immunity antagonist in several CoVs, including mouse hepatitis virus (MHV) and severe acute respiratory syndrome (SARS)-CoV. However, the underlying molecular mechanism(s) remain unclear. In this study, we found that MHV N protein inhibited Sendai virus and poly(I:C)-induced IFN-β production by targeting a molecule upstream of retinoic acid-induced gene I (RIG-I) and melanoma differentiation gene 5 (MDA5). Further studies showed that both MHV and SARS-CoV N proteins directly interacted with protein activator of protein kinase R (PACT), a cellular dsRNA-binding protein that can bind to RIG-I and MDA5 to activate IFN production. The N–PACT interaction sequestered the association of PACT and RIG-I/MDA5, which in turn inhibited IFN-β production. However, the N proteins from porcine epidemic diarrhea virus (PEDV) and porcine reproductive and respiratory syndrome virus (PRRSV), which are also classified in the order Nidovirales, did not interact and counteract with PACT. Taken together, our present study confirms that both MHV and SARS-CoV N proteins can perturb the function of cellular PACT to circumvent the innate antiviral response. However, this strategy does not appear to be used by all CoVs N proteins.
has issue date	2017-05-17(xsd:dateTime)
bibo:doi	10.18632/oncotarget.17912
bibo:pmid	28591694
has license	cc-by
sha1sum (hex)	9b8a2314912eaeb1c509cf88492f463148a0a9ed
schema:url	https://doi.org/10.18632/oncotarget.17912
resource representing a document's title	The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/MDA5 activation
has PubMed Central identifier	PMC5564796
has PubMed identifier	28591694
schema:publication	Oncotarget
resource representing a document's body	covid:9b8a2314912eaeb1c509cf88492f463148a0a9ed#body_text
is schema:about of	named entity 'MDA5' named entity 'ATTENUATION' covid:arg/9b8a2314912eaeb1c509cf88492f463148a0a9ed named entity 'VIRAL PROTEIN' named entity 'IDENTIFIED' named entity 'INHIBITED' named entity 'ANTAGONIST' named entity 'PRODUCTION' named entity 'ABUNDANT' named entity 'INDUCED' named entity 'MOUSE HEPATITIS VIRUS' named entity 'COVS' named entity 'UNDERLYING' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' named entity 'SENDAI VIRUS' named entity 'INNATE IMMUNITY' named entity 'PROTEIN ' named entity 'MOLECULE' named entity 'IFN' named entity 'MEDIATED' named entity 'RIG-I' named entity 'SHARE' named entity 'MECHANISM' named entity 'NUCLEOCAPSID PROTEINS' named entity 'MDA5' named entity 'MOUSE HEPATITIS VIRUS' named entity 'PACT' named entity 'IFN' named entity 'CELLS' named entity 'INFECTED' named entity '28S' named entity '28I' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'UNCLEAR' named entity 'TARGETING' named entity 'MOLECULAR MECHANISM' named entity 'ACTIVATION' named entity 'STUDY' named entity 'N PROTEIN' named entity 'FOUND' named entity 'POLY' named entity 'INCLUDING' named entity 'immunity' named entity 'Sendai' named entity 'remain' named entity 'poly' named entity 'identified' named entity 'RIG-I' named entity 'virus' named entity 'innate immunity' named entity 'protein' named entity 'viral protein' named entity 'severe acute respiratory syndrome coronavirus' named entity 'mouse hepatitis virus' named entity 'IFN' named entity 'protein' named entity 'protein' named entity 'mRNA' named entity 'arteriviridae' named entity 'CoV' named entity 'plasmids' named entity 'oncotarget' named entity 'Nucleocapsid' named entity 'Primer' named entity '293T' named entity 'RIG-I' named entity 'SARS-CoV' named entity 'GAPDH' named entity 'innate immune' named entity 'IFN' named entity 'SARS-CoV' named entity 'severe acute respiratory syndrome coronavirus'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software