About: Host cell proteins interacting with the 3′ end of TGEV coronavirus genome influence virus replication

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

About: Host cell proteins interacting with the 3′ end of TGEV coronavirus genome influence virus replication Goto Sponge NotDistinct Permalink

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
has title	Host cell proteins interacting with the 3′ end of TGEV coronavirus genome influence virus replication
Creator	Enjuanes, Luis Sola, Isabel Nogales, Aitor Almazán, Fernando Galán, Carmen Akoulitchev, Alexandre Thomas, Benjamin
Source	Elsevier; Medline; PMC
abstract	Abstract Coronavirus RNA synthesis is performed by a multienzymatic replicase complex together with cellular factors. This process requires the specific recognition of RNA cis-acting signals located at the ends of the viral genome. To identify cellular proteins involved in coronavirus RNA synthesis, transmissible gastroenteritis coronavirus (TGEV) genome ends, harboring essential cis-acting signals for replication, were used as baits for RNA affinity protein purification. Ten proteins were preferentially pulled down with either the 5′ or 3′ ends of the genome and identified by proteomic analysis. Nine of them, including members of the heterogeneous ribonucleoprotein family of proteins (hnRNPs), the poly(A)-binding protein (PABP), the p100 transcriptional co-activator protein and two aminoacyl-tRNA synthetases, showed a preferential binding to the 3′ end of the genome, whereas only the polypyrimidine tract-binding protein (PTB) was preferentially pulled down with the 5′ end of the genome. The potential function of the 3′ end-interacting proteins in virus replication was studied by analyzing the effect of their silencing using a TGEV-derived replicon and the infectious virus. Gene silencing of PABP, hnRNP Q, and glutamyl-prolyl-tRNA synthetase (EPRS) caused a significant 2 to 3-fold reduction of viral RNA synthesis. Interestingly, the silencing of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), initially used as a control gene, caused a 2 to 3-fold increase in viral RNA synthesis in both systems. These data suggest that PABP, hnRNP Q, and EPRS play a positive role in virus infection that could be mediated through their interaction with the viral 3′ end, and that GAPDH has a negative effect on viral infection.
has issue date	2009-09-01(xsd:dateTime)
bibo:doi	10.1016/j.virol.2009.06.006
bibo:pmid	19580983
has license	els-covid
sha1sum (hex)	a40ffc155e4d5c385e7a1fe04010a9b5469c7753
schema:url	https://doi.org/10.1016/j.virol.2009.06.006
resource representing a document's title	Host cell proteins interacting with the 3′ end of TGEV coronavirus genome influence virus replication
has PubMed Central identifier	PMC7118768
has PubMed identifier	19580983
schema:publication	Virology
resource representing a document's body	covid:a40ffc155e4d5c385e7a1fe04010a9b5469c7753#body_text
is schema:about of	named entity 'caused' named entity 'signals' named entity 'initially' named entity 'pulled' named entity 'ribonucleoprotein' named entity 'This' named entity 'GAPDH' named entity 'involved' named entity 'ends' named entity 'replication' named entity 'influence' covid:arg/a40ffc155e4d5c385e7a1fe04010a9b5469c7753 named entity 'virus' named entity 'protein purification' named entity 'synthetase' named entity 'PTB' named entity 'infection' named entity 'RNA' named entity 'studied' named entity 'proteomic' named entity 'nuclear factors' named entity 'titer' named entity 'amplicon' named entity 'replicon' named entity 'transfected' named entity 'TGEV' named entity 'virus' named entity 'positive control' named entity 'PABP' named entity 'inoculum' named entity '10 nM' named entity 'viral RNA' named entity 'deionized water' named entity 'siRNAs' named entity 'RNA' named entity 'siRNAs' named entity 'RNA' named entity 'glyceraldehyde 3-phosphate dehydrogenase' named entity 'Mung Bean nuclease' named entity 'envelope protein' named entity 'genome' named entity 'University of Oxford' named entity 'Immobilon' named entity 'testis' named entity 'Cy3' named entity '5′ end' named entity 'RNA processing' named entity 'significant effect' named entity 'positive control' named entity 'affinity chromatography' named entity 'mRNA' named entity 'Elmen' named entity 'TGEV' named entity 'protein' named entity 'replicase' named entity 'MASCOT' named entity 'hybridoma' named entity 'mRNA' named entity 'negative control' named entity 'ethanol precipitation' named entity 'formic acid' named entity 'Applied Biosystems' named entity 'negative control' named entity 'replicon' named entity 'exoribonuclease' named entity 'siRNAs' named entity 'RNA' named entity 'TGEV' named entity 'time-of-flight mass spectrometry' named entity 'restriction sites' named entity 'protein' named entity 'transfected' named entity 'siRNAs' named entity 'loading control' named entity 'protein'

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 © 2009-2024 OpenLink Software