About: Nuclear imprisonment of host cellular mRNA by nsp1β protein of porcine reproductive and respiratory syndrome virus

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About: Nuclear imprisonment of host cellular mRNA by nsp1β protein of porcine reproductive and respiratory syndrome virus Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Nuclear imprisonment of host cellular mRNA by nsp1β protein of porcine reproductive and respiratory syndrome virus
Creator	Han, Mingyuan Yoo, Dongwan Ke, Hanzhong Zhang, Qingzhan
Source	Elsevier; Medline; PMC
abstract	Abstract Positive-strand RNA genomes function as mRNA for viral protein synthesis which is fully reliant on host cell translation machinery. Competing with cellular protein translation apparatus needs to ensure the production of viral proteins, but this also stifles host innate defense. In the present study, we showed that porcine reproductive and respiratory syndrome virus (PRRSV), whose replication takes place in the cytoplasm, imprisoned host cell mRNA in the nucleus, which suggests a novel mechanism to enhance translation of PRRSV genome. PRRSV nonstructural protein (nsp) 1β was identified as the nuclear protein playing the role for host mRNA nuclear retention and subversion of host protein synthesis. A SAP (SAF-A/B, Acinus, and PIAS) motif was identified in nsp1β with the consensus sequence of 126-LQxxLxxxGL-135. In situ hybridization unveiled that SAP mutants were unable to cause nuclear retention of host cell mRNAs and did not suppress host protein synthesis. In addition, these SAP mutants reverted PRRSV-nsp1β-mediated suppression of interferon (IFN) production, IFN signaling, and TNF-α production pathway. Using reverse genetics, a series of SAP mutant PRRS viruses, vK124A, vL126A, vG134A, and vL135A were generated. No mRNA nuclear retention was observed during vL126A and vL135A infections. Importantly, vL126A and vL135A did not suppress IFN production. For other arteriviruses, mRNA nuclear accumulation was also observed for LDV-nsp1β and SHFV-nsp1β. EAV-nsp1 was exceptional and did not block the host mRNA nuclear export.
has issue date	2017-05-31(xsd:dateTime)
bibo:doi	10.1016/j.virol.2017.02.004
bibo:pmid	28235682
has license	els-covid
sha1sum (hex)	e4298a045d0f84255373669f860245c982c25e1c
schema:url	https://doi.org/10.1016/j.virol.2017.02.004
resource representing a document's title	Nuclear imprisonment of host cellular mRNA by nsp1β protein of porcine reproductive and respiratory syndrome virus
has PubMed Central identifier	PMC7111332
has PubMed identifier	28235682
schema:publication	Virology
resource representing a document's body	covid:e4298a045d0f84255373669f860245c982c25e1c#body_text
is schema:about of	named entity 'CELLULAR' named entity 'virus' named entity 'SAP' named entity 'TNF-' named entity '2FB' named entity 'NUCLEAR EXPORT' named entity 'INFECTIONS' named entity 'MEDIATED' named entity 'CYTOPLASM' named entity 'NOVEL' named entity 'APPARATUS' named entity 'PRESENT' named entity 'THESE' named entity '135' named entity 'FUNCTION' named entity 'NSP1' named entity 'SERIES' named entity 'SIGNALING' named entity 'STIFLES' named entity 'IFN' named entity 'REPLICATION' named entity 'ADDITION' named entity 'CONSENSUS SEQUENCE' named entity 'CAUSE' named entity 'NUCLEAR' named entity '126' named entity 'PROTEIN TRANSLATION' named entity 'ENHANCE' named entity 'HOST CELL' named entity 'ROLE' named entity 'ENSURE' named entity 'IN SITU HYBRIDIZATION' named entity 'MACHINERY' named entity 'MECHANISM' named entity 'PRRS' named entity 'NEEDS' named entity 'STRAND' named entity 'OBSERVED' named entity 'ACINUS' named entity 'HOST' named entity 'SUPPRESSION' named entity 'FULLY' named entity 'MUTANT' named entity 'BLOCK' named entity 'INTERFERON ' named entity 'PLAYING' named entity 'STUDY' named entity 'DID' named entity 'BUT' named entity 'REVERSE GENETICS' named entity 'SUPPRESS' named entity 'SAP' named entity 'HOST PROTEIN' named entity 'PIAS' named entity 'MOTIF' named entity 'CELLULAR' named entity 'PROTEIN SYNTHESIS' named entity 'GENOME' named entity 'MUTANTS' named entity 'POSITIVE' named entity 'RNA' named entity 'MRNA' named entity 'VIRAL PROTEIN SYNTHESIS' named entity 'RETENTION' named entity 'HOST' named entity 'IMPRISONMENT' named entity 'MRNA' named entity 'NUCLEAR' named entity 'ACCUMULATION' named entity 'IDENTIFIED' named entity 'EAV' named entity 'GENERATED' named entity 'NUCLEAR PROTEIN' named entity 'PRODUCTION' named entity 'TRANSLATION' named entity 'NUCLEUS' named entity 'PROTEIN ' named entity 'VIRUSES'

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