About: Ubiquitination Is Required for Effective Replication of Coxsackievirus B3

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

About: Ubiquitination Is Required for Effective Replication of Coxsackievirus B3 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	Ubiquitination Is Required for Effective Replication of Coxsackievirus B3
Creator	Luo, Honglin Gao, Guang Si, Xiaoning Wang, Yahong Wong, Jerry Zhang, Jingchun
topic	covid:9e45efb86c7c552be221e4d1356d9374a7ebc204#this
Source	PMC
abstract	BACKGROUND: Protein ubiquitination and/or degradation by the ubiquitin/proteasome system (UPS) have been recognized as critical mechanisms in the regulation of numerous essential cellular functions. The importance of the UPS in viral pathogenesis has become increasingly apparent. Using murine cardiomyocytes, we have previously demonstrated that the UPS plays a key role in the replication of coxsackievirus B3 (CVB3), an important human pathogen associated with various diseases. To further elucidate the underlying mechanisms, we examined the interplay between the UPS and CVB3, focusing on the role of ubiquitination in viral lifecycle. METHODOLOGY/PRINCIPAL FINDINGS: As assessed by in situ hybridization, Western blot, and plaque assay, we showed that proteasome inhibition decreased CVB3 RNA replication, protein synthesis, and viral titers in HeLa cells. There were no apparent changes in 20S proteasome activities following CVB3 infection. However, we found viral infection led to an accumulation of protein-ubiquitin conjugates, accompanied by a decreased protein expression of free ubiquitin, implicating an important role of ubiquitination in the UPS-mediated viral replication. Using small-interfering RNA, we demonstrated that gene-silencing of ubiquitin significantly reduced viral titers, possibly through downregulation of protein ubiquitination and subsequent alteration of protein function and/or degradation. Inhibition of deubiquitinating enzymes apparently enhances the inhibitory effects of proteasome inhibitors on CVB3 replication. Finally, by immunoprecipitation, we showed that coxsackieviral polymerase 3D was post-translationally modified by ubiquitination and such modification might be a prerequisite for its function in transcriptional regulation of viral genome. CONCLUSION: Coxsackievirus infection promotes protein ubiquitination, contributing to effective viral replication, probably through ubiquitin modification of viral polymerase.
has issue date	2008-07-09(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0002585
bibo:pmid	18612413
has license	cc-by
sha1sum (hex)	9e45efb86c7c552be221e4d1356d9374a7ebc204
schema:url	https://doi.org/10.1371/journal.pone.0002585
resource representing a document's title	Ubiquitination Is Required for Effective Replication of Coxsackievirus B3
has PubMed Central identifier	PMC2440516
has PubMed identifier	18612413
schema:publication	PLoS One
resource representing a document's body	covid:9e45efb86c7c552be221e4d1356d9374a7ebc204#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/9e45efb86c7c552be221e4d1356d9374a7ebc204
is schema:about of	named entity 'VIRAL' named entity 'PROTEIN UBIQUITINATION' named entity 'VARIOUS' named entity 'UBIQUITINATION' named entity 'USING' named entity 'COXSACKIEVIRUS B3' named entity 'UPS' named entity 'ROLE' named entity 'UNDERLYING' named entity 'UBIQUITIN' named entity 'ASSOCIATED WITH' named entity 'PREVIOUSLY' named entity 'REGULATION' named entity 'NUMEROUS' named entity 'DEMONSTRATED' named entity 'DISEASES' named entity 'BACKGROUND' named entity 'PLAYS' named entity 'PATHOGEN' named entity 'DEGRADATION' covid:arg/9e45efb86c7c552be221e4d1356d9374a7ebc204 named entity 'COXSACKIEVIRUS B3' named entity 'EFFECTIVE' named entity 'REQUIRED' named entity 'UBIQUITINATION' named entity 'REPLICATION' named entity 'CARDIOMYOCYTES' named entity 'HUMAN' named entity 'IMPORTANT' named entity 'APPARENT' named entity 'REPLICATION' named entity 'EXAMINED' named entity 'FOCUSING' named entity 'MURINE' named entity 'SYSTEM' named entity 'KEY' named entity 'FUNCTIONS' named entity 'HAVE' named entity 'CRITICAL' named entity 'MECHANISMS' named entity 'CELLULAR' named entity 'ESSENTIAL' named entity 'VIRAL PATHOGENESIS' named entity 'cellular' named entity 'UPS' named entity 'coxsackievirus' named entity 'key' named entity 'ubiquitin/proteasome' named entity 'Coxsackievirus B3' named entity 'ubiquitin' named entity 'chromatin remodeling' named entity 'protein' named entity 'murine' named entity 'infection' named entity 'cell death' named entity 'EDTA' named entity 'HeLa' named entity 'viral replication' named entity 'protein degradation' named entity 'PBS' named entity 'infection' named entity 'proteasome inhibitor' named entity 'serially diluted' named entity 'UPS' named entity 'deubiquitinating' named entity 'protein' named entity 'ubiquitination' named entity 'Carnoy' named entity 'antibody' named entity 'Virus' named entity 'cyclin-dependent kinases' named entity 'picornaviridae' named entity 'dry milk' named entity 'ubiquitination'

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