About: Human Respiratory Syncytial Virus NS 1 Targets TRIM25 to Suppress RIG-I Ubiquitination and Subsequent RIG-I-Mediated Antiviral Signaling

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About: Human Respiratory Syncytial Virus NS 1 Targets TRIM25 to Suppress RIG-I Ubiquitination and Subsequent RIG-I-Mediated Antiviral Signaling 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	Human Respiratory Syncytial Virus NS 1 Targets TRIM25 to Suppress RIG-I Ubiquitination and Subsequent RIG-I-Mediated Antiviral Signaling
Creator	Ban, Junsu Inn, Kyung-Soo Lee, Na-Rae Lee, Noh-Jin Quan, Fu-Shi Lee, Jong
Source	Medline; PMC
abstract	Respiratory syncytial virus (RSV) causes severe acute lower respiratory tract disease. Retinoic acid-inducible gene-I (RIG-I) serves as an innate immune sensor and triggers antiviral responses upon recognizing viral infections including RSV. Since tripartite motif-containing protein 25 (TRIM25)-mediated K63-polyubiquitination is crucial for RIG-I activation, several viruses target initial RIG-I activation through ubiquitination. RSV NS1 and NS2 have been shown to interfere with RIG-I-mediated antiviral signaling. In this study, we explored the possibility that NS1 suppresses RIG-I-mediated antiviral signaling by targeting TRIM25. Ubiquitination of ectopically expressed RIG-I-2Cards domain was decreased by RSV infection, indicating that RSV possesses ability to inhibit TRIM25-mediated RIG-I ubiquitination. Similarly, ectopic expression of NS1 sufficiently suppressed TRIM25-mediated RIG-I ubiquitination. Furthermore, interaction between NS1 and TRIM25 was detected by a co-immunoprecipitation assay. Further biochemical assays showed that the SPRY domain of TRIM25, which is responsible for interaction with RIG-I, interacted sufficiently with NS1. Suppression of RIG-I ubiquitination by NS1 resulted in decreased interaction between RIG-I and its downstream molecule, MAVS. The suppressive effect of NS1 on RIG-I signaling could be abrogated by overexpression of TRIM25. Collectively, this study suggests that RSV NS1 interacts with TRIM25 and interferes with RIG-I ubiquitination to suppress type-I interferon signaling.
has issue date	2018-12-14(xsd:dateTime)
bibo:doi	10.3390/v10120716
bibo:pmid	30558248
has license	cc-by
sha1sum (hex)	45d3b6128146d7df335e96fb8257644f0a5fca14
schema:url	https://doi.org/10.3390/v10120716
resource representing a document's title	Human Respiratory Syncytial Virus NS 1 Targets TRIM25 to Suppress RIG-I Ubiquitination and Subsequent RIG-I-Mediated Antiviral Signaling
has PubMed Central identifier	PMC6316657
has PubMed identifier	30558248
schema:publication	Viruses
resource representing a document's body	covid:45d3b6128146d7df335e96fb8257644f0a5fca14#body_text
is schema:about of	named entity 'RIG-I' named entity 'SUPPRESS' named entity 'EXPRESSED' named entity 'SUBSEQUENT' named entity 'VIRAL INFECTIONS' named entity 'TARGET' named entity 'POLYUBIQUITINATION' named entity 'TRIGGERS' named entity 'ANTIVIRAL' named entity 'ANTIVIRAL' named entity 'INTERACTION' named entity 'RIG-I' named entity 'MAVS' named entity 'SUPPRESSED' named entity 'LOWER RESPIRATORY TRACT DISEASE' named entity 'SUPPRESSIVE EFFECT' named entity 'UBIQUITINATION' named entity 'INTERFERE' named entity 'SIGNALING' named entity 'RSV INFECTION' named entity 'IMMUNE' named entity 'SUPPRESSES' named entity 'STUDY' named entity 'HUMAN RESPIRATORY SYNCYTIAL VIRUS' named entity 'MEDIATED' named entity 'RESPIRATORY SYNCYTIAL VIRUS' named entity 'TRIM25' named entity 'TARGETING' named entity 'SPRY DOMAIN' named entity 'TRIM25' named entity 'SIGNALING' named entity 'UBIQUITINATION' named entity 'MEDIATED' named entity 'HAVE' named entity 'DECREASED BY' named entity 'COULD BE' named entity 'CO-IMMUNOPRECIPITATION ASSAY' named entity 'ECTOPIC EXPRESSION' named entity 'INDICATING' named entity 'DETECTED' named entity 'INDUCIBLE' named entity 'RESPONSES' named entity 'RSV' named entity 'SUPPRESSION' named entity 'DOWNSTREAM' named entity 'SEVERE' named entity 'VIRUSES' named entity 'TO INHIBIT' named entity 'POSSIBILITY' named entity 'DOMAIN' named entity 'NS1' named entity 'ITS' named entity 'RESPONSIBLE' named entity 'GENE' named entity 'ACUTE' named entity 'NS2' named entity 'TRIPARTITE MOTIF-CONTAINING PROTEIN 25' named entity 'BIOCHEMICAL' named entity 'CAUSES' named entity 'INITIAL' named entity 'TARGETS' named entity 'ACTIVATION' named entity 'DECREASED' named entity 'OVEREXPRESSION' named entity 'POSSESSES' named entity 'SENSOR' named entity 'INTERFERES WITH' named entity 'SUPPRESS' named entity 'K63' named entity 'RETINOIC ACID' named entity 'INCLUDING' named entity 'TYPE' named entity 'MOLECULE' named entity 'INTERFERON SIGNALING' covid:arg/45d3b6128146d7df335e96fb8257644f0a5fca14 named entity 'ectopically expressed'

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