About: eEF1A Interacts with the NS5A Protein and Inhibits the Growth of Classical Swine Fever Virus

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About: eEF1A Interacts with the NS5A Protein and Inhibits the Growth of Classical Swine Fever Virus 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	eEF1A Interacts with the NS5A Protein and Inhibits the Growth of Classical Swine Fever Virus
Creator	Li, Su Feng, Shuo Dong, Hong He, Wen-Rui Li, Lian-Feng Li, Yongfeng Qin, Hua-Yang Qiu, Hua-Ji Wang, Jing-Han Yu, Shao-Xiong
Source	Medline; PMC
abstract	The NS5A protein of classical swine fever virus (CSFV) is involved in the RNA synthesis and viral replication. However, the NS5A-interacting cellular proteins engaged in the CSFV replication are poorly defined. Using yeast two-hybrid screen, the eukaryotic elongation factor 1A (eEF1A) was identified to be an NS5A-binding partner. The NS5A–eEF1A interaction was confirmed by coimmunoprecipitation, glutathione S-transferase (GST) pulldown and laser confocal microscopy assays. The domain I of eEF1A was shown to be critical for the NS5A–eEF1A interaction. Overexpression of eEF1A suppressed the CSFV growth markedly, and conversely, knockdown of eEF1A enhanced the CSFV replication significantly. Furthermore, eEF1A, as well as NS5A, was found to reduce the translation efficiency of the internal ribosome entry site (IRES) of CSFV in a dose-dependent manner, as demonstrated by luciferase reporter assay. Streptavidin pulldown assay revealed that eEF1A could bind to the CSFV IRES. Collectively, our results suggest that eEF1A interacts with NS5A and negatively regulates the growth of CSFV.
has issue date	2015-08-10(xsd:dateTime)
bibo:doi	10.3390/v7082833
bibo:pmid	26266418
has license	cc-by
sha1sum (hex)	f793bcacac81ad9341709c9351c6c40c49f4c52e
schema:url	https://doi.org/10.3390/v7082833
resource representing a document's title	eEF1A Interacts with the NS5A Protein and Inhibits the Growth of Classical Swine Fever Virus
has PubMed Central identifier	PMC4576194
has PubMed identifier	26266418
schema:publication	Viruses
resource representing a document's body	covid:f793bcacac81ad9341709c9351c6c40c49f4c52e#body_text
is schema:about of	named entity 'replication' named entity 'virus' named entity 'RNA' named entity 'elongation factor' named entity 'Virus' named entity 'GLUTATHIONE S-TRANSFERASE' named entity 'REVEALED' named entity 'RNA SYNTHESIS' named entity 'CONFOCAL MICROSCOPY' named entity 'YEAST TWO-HYBRID' named entity 'NS5A PROTEIN' named entity 'CELLULAR' named entity 'SCREEN' named entity 'CLASSICAL SWINE FEVER VIRUS' named entity 'DOMAIN' named entity 'GROWTH' named entity 'LUCIFERASE' named entity 'FOUND' named entity 'PROTEIN ' named entity 'EEF1A' named entity 'CLASSICAL SWINE FEVER VIRUS' named entity 'ELONGATION FACTOR' named entity 'DOSE-DEPENDENT' named entity 'SUPPRESSED' named entity 'PULLDOWN' named entity 'LASER' named entity 'INTERACTING' named entity 'USING' named entity 'INTERACTION' named entity 'SUGGEST' named entity 'PROTEINS' named entity 'RESULTS' named entity 'ENHANCED' named entity 'STREPTAVIDIN' named entity 'CONFIRMED BY' named entity 'BINDING' named entity 'OVEREXPRESSION' named entity 'INTERNAL RIBOSOME ENTRY SITE' named entity 'EUKARYOTIC' named entity 'TRANSLATION' named entity 'EFFICIENCY' named entity 'PARTNER' named entity 'VIRAL REPLICATION' named entity 'EEF1A' named entity 'ASSAY' named entity 'TO REDUCE' named entity 'REPORTER ASSAY' named entity 'PROTEIN ' named entity 'CRITICAL' named entity 'IDENTIFIED' named entity 'COIMMUNOPRECIPITATION' named entity 'OUR' named entity 'IRES' named entity 'GROWTH' named entity 'NS5A' named entity 'NS5A PROTEIN' named entity 'ENGAGED' named entity 'MARKEDLY' named entity 'BIND' named entity 'POORLY DEFINED' named entity 'REPLICATION' named entity 'INVOLVED' covid:arg/f793bcacac81ad9341709c9351c6c40c49f4c52e named entity 'However' named entity 'CSFV' named entity 'lentiviruses' named entity 'CSFV' named entity 'Coimmunoprecipitation' named entity 'eEF1A' named entity 'IRES' named entity 'Pestivirus' named entity 'MOI'

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