About: dsRNA binding characterization of full length recombinant wild type and mutants Zaire ebolavirus VP35

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

About: dsRNA binding characterization of full length recombinant wild type and mutants Zaire ebolavirus VP35 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
title	dsRNA binding characterization of full length recombinant wild type and mutants Zaire ebolavirus VP35
Creator	Tramontano, Enzo Zinzula, Luca Esposito, Francesca Pala, Daniela
topic	covid:0de2eeac8443a36c67b0d8e17872a3ce56a6471f#this
source	Elsevier; Medline; PMC
abstract	Abstract The Ebola viruses (EBOVs) VP35 protein is a multifunctional major virulence factor involved in EBOVs replication and evasion of the host immune system. EBOV VP35 is an essential component of the viral RNA polymerase, it is a key participant of the nucleocapsid assembly and it inhibits the innate immune response by antagonizing RIG-I like receptors through its dsRNA binding function and, hence, by suppressing the host type I interferon (IFN) production. Insights into the VP35 dsRNA recognition have been recently revealed by structural and functional analysis performed on its C-terminus protein. We report the biochemical characterization of the Zaire ebolavirus (ZEBOV) full-length recombinant VP35 (rVP35)–dsRNA binding function. We established a novel in vitro magnetic dsRNA binding pull down assay, determined the rVP35 optimal dsRNA binding parameters, measured the rVP35 equilibrium dissociation constant for heterologous in vitro transcribed dsRNA of different length and short synthetic dsRNA of 8bp, and validated the assay for compound screening by assessing the inhibitory ability of auryntricarboxylic acid (IC50 value of 50μg/mL). Furthermore, we compared the dsRNA binding properties of full length wt rVP35 with those of R305A, K309A and R312A rVP35 mutants, which were previously reported to be defective in dsRNA binding-mediated IFN inhibition, showing that the latter have measurably increased K d values for dsRNA binding and modified migration patterns in mobility shift assays with respect to wt rVP35. Overall, these results provide the first characterization of the full-length wt and mutants VP35–dsRNA binding functions.
has issue date	2012-03-31(xsd:dateTime)
bibo:doi	10.1016/j.antiviral.2012.01.005
bibo:pmid	22289166
has license	els-covid
sha1sum (hex)	0de2eeac8443a36c67b0d8e17872a3ce56a6471f
schema:url	https://doi.org/10.1016/j.antiviral.2012.01.005
resource representing a document's title	dsRNA binding characterization of full length recombinant wild type and mutants Zaire ebolavirus VP35
has PubMed Central identifier	PMC7114247
has PubMed identifier	22289166
schema:publication	Antiviral Research
resource representing a document's body	covid:0de2eeac8443a36c67b0d8e17872a3ce56a6471f#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/0de2eeac8443a36c67b0d8e17872a3ce56a6471f
is schema:about of	named entity 'VP35' named entity 'dissociation constant' named entity 'key' named entity 'C-terminus' named entity 'EBOV' named entity 'equilibrium' named entity 'IFN' named entity 'synthetic' named entity 'length' named entity 'binding' named entity 'type I interferon' named entity 'viruses' named entity 'heterologous' named entity 'dsRNA' named entity 'compound' named entity 'recombinant' named entity 'recombinant' named entity 'MAGNETIC' named entity 'PROTEIN' named entity 'REPLICATION' named entity 'VALUE' named entity 'VALIDATED' named entity 'PRODUCTION' named entity 'DIFFERENT' named entity 'RECENTLY' named entity 'RIG-I LIKE RECEPTORS' named entity 'DSRNA BINDING' named entity 'MAJOR' named entity 'RECOGNITION' named entity 'REVEALED' named entity 'SHORT' named entity 'INVOLVED' named entity 'COMPOUND' named entity 'BINDING FUNCTION' named entity 'CHARACTERIZATION' named entity 'MUTANTS' named entity 'REPORTED' named entity 'INHIBITORY' named entity 'INHIBITION' named entity 'VP35' named entity 'HOST' named entity 'ESSENTIAL' named entity 'ACID' named entity 'COMPARED' named entity 'NUCLEOCAPSID' named entity 'VALUES' named entity 'INTERFERON ' named entity 'IFN' named entity 'PARAMETERS' named entity 'ASSESSING' named entity 'PROPERTIES' named entity 'RESULTS' named entity 'RNA POLYMERASE' named entity 'HAVE' named entity 'RECOMBINANT' named entity 'DSRNA' named entity 'SUPPRESSING' named entity 'VIRUSES' named entity 'VIRULENCE FACTOR' named entity 'ASSEMBLY' named entity 'IN VITRO' named entity 'ABILITY' named entity 'PREVIOUSLY' named entity 'VIRAL RNA' named entity 'HETEROLOGOUS' named entity 'ANALYSIS PERFORMED' named entity 'LENGTH' named entity 'MOBILITY SHIFT ASSAYS' named entity 'TRANSCRIBED' named entity 'MIGRATION' named entity 'DETERMINED' named entity 'INSIGHTS' named entity 'PATTERNS' named entity 'REPORT' named entity 'INCREASED' named entity 'MUTANTS'

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