About: The Ebola Virus Nucleoprotein Recruits the Nuclear RNA Export Factor NXF1 into Inclusion Bodies to Facilitate Viral Protein Expression

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About: The Ebola Virus Nucleoprotein Recruits the Nuclear RNA Export Factor NXF1 into Inclusion Bodies to Facilitate Viral Protein Expression 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	The Ebola Virus Nucleoprotein Recruits the Nuclear RNA Export Factor NXF1 into Inclusion Bodies to Facilitate Viral Protein Expression
Creator	Hoenen, Thomas Brandt, Janine Reiche, Sven Traeger, Shelby Wendt, Lisa Bodmer, Bianca Schmidt, Marie
Source	PMC
abstract	Ebola virus (EBOV) causes severe outbreaks of viral hemorrhagic fever in humans. While virus-host interactions are promising targets for antivirals, there is only limited knowledge regarding the interactions of EBOV with cellular host factors. Recently, we performed a genome-wide siRNA screen that identified the nuclear RNA export factor 1 (NXF1) as an important host factor for the EBOV life cycle. NXF1 is a major component of the nuclear mRNA export pathway that is usurped by many viruses whose life cycles include nuclear stages. However, the role of NXF1 in the life cycle of EBOV, a virus replicating in cytoplasmic inclusion bodies, remains unknown. In order to better understand the role of NXF1 in the EBOV life cycle, we performed a combination of co-immunoprecipitation and double immunofluorescence assays to characterize the interactions of NXF1 with viral proteins and RNAs. Additionally, using siRNA-mediated knockdown of NXF1 together with functional assays, we analyzed the role of NXF1 in individual aspects of the virus life cycle. With this approach we identified the EBOV nucleoprotein (NP) as a viral interaction partner of NXF1. Further studies revealed that NP interacts with the RNA-binding domain of NXF1 and competes with RNA for this interaction. Co-localization studies showed that RNA binding-deficient, but not wildtype NXF1, accumulates in NP-derived inclusion bodies, and knockdown experiments demonstrated that NXF1 is necessary for viral protein expression, but not for viral RNA synthesis. Finally, our results showed that NXF1 interacts with viral mRNAs, but not with viral genomic RNAs. Based on these results we suggest a model whereby NXF1 is recruited into inclusion bodies to promote the export of viral mRNA:NXF1 complexes from these sites. This would represent a novel function for NXF1 in the life cycle of cytoplasmically replicating viruses, and may provide a basis for new therapeutic approaches against EBOV, and possibly other emerging viruses.
has issue date	2020-01-11(xsd:dateTime)
bibo:doi	10.3390/cells9010187
bibo:pmid	31940815
has license	cc-by
sha1sum (hex)	a068f1ec98befb3d767ba602df5f314604f0aee8
schema:url	https://doi.org/10.3390/cells9010187
resource representing a document's title	The Ebola Virus Nucleoprotein Recruits the Nuclear RNA Export Factor NXF1 into Inclusion Bodies to Facilitate Viral Protein Expression
has PubMed Central identifier	PMC7017048
has PubMed identifier	31940815
schema:publication	Cells
resource representing a document's body	covid:a068f1ec98befb3d767ba602df5f314604f0aee8#body_text
is schema:about of	named entity 'NXF1' named entity 'wildtype' named entity 'interactions' named entity 'EBOV' named entity 'inclusion bodies' named entity 'nucleoprotein' named entity 'proteins' named entity 'siRNA' named entity 'NXF1' named entity 'While' named entity 'RNA' named entity 'interacts' covid:arg/a068f1ec98befb3d767ba602df5f314604f0aee8 named entity 'viruses' named entity 'EBOV' named entity 'identified' named entity 'export' named entity 'identified' named entity 'cellular' named entity 'mRNA' named entity 'deletion mutants' named entity 'binding domain' named entity 'RNase' named entity 'L-1000' named entity 'plasmid' named entity 'NXF1' named entity 'Western blot' named entity 'NXF1' named entity 'NXF1' named entity 'RNA binding' named entity 'NXF1' named entity 'mRNAs' named entity 'vector' named entity 'RBD' named entity 'Alexa Fluor' named entity 'viral protein' named entity 'inclusion bodies' named entity 'Hepatitis B virus' named entity 'viral proteins' named entity 'NXF1' named entity 'antibodies' named entity 'VP40' named entity 'interactions' named entity 'represent' named entity 'export' named entity 'individual' named entity 'viral hemorrhagic fever' named entity 'NXF1' named entity 'studies' named entity 'NXF1' named entity 'RNAs' named entity 'emerging viruses' named entity 'NXF1' named entity 'nucleoprotein' named entity 'viral proteins' named entity 'RNA-binding' named entity 'EBOV' named entity 'EBOV' named entity 'NXF1' named entity 'life cycle' named entity 'NXF1' named entity 'EBOV' named entity 'NXF1' named entity 'virus' named entity 'antivirals' named entity 'EBOV' named entity 'NXF1' named entity 'lysate' named entity 'inclusion bodies' named entity 'NXF1' named entity 'NXF1' named entity 'NXF1' named entity 'biochemical' named entity 'PBS' named entity 'inclusion bodies'

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