Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Involvement of the zinc-binding capacity of Sendai virus V protein in viral pathogenesis.
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The V-unique C-terminal domain of Sendai virus V binds zinc, and the binding depends on seven conserved cysteine residues.
"GST-Vu bound 7.2-fold more zinc than did GST, exhibiting its potential zinc-binding capacity"
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Recombinant viruses carrying single cysteine substitutions that impair zinc binding replicate normally in cultured cells but are strongly attenuated in mice, so the zinc site is required for pathogenicity rather than for replication.
"the mutant viruses were strongly attenuated in mice"
C and V proteins of Sendai virus target signaling pathways leading to IRF-3 activation for the negative regulation of interferon-beta production.
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Independently expressed V inhibits double-stranded RNA- and Newcastle disease virus-induced activation of IRF-3 and of the interferon-beta promoter.
"C or V inhibited the double-stranded (ds) RNA- or Newcastle disease virus"
Inhibition of interferon regulatory factor 3 activation by paramyxovirus V protein.
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Expressed V protein is dispersed through the host cytosol, whereas the Vu fragment is found in both cytosol and nucleus.
"When only the V protein was expressed, it appeared to be dispersed in the cytosol."
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V co-immunoprecipitates with host RIG-I, MDA5 and IRF3, and with the constitutively active IRF3-5D.
"Here we reproduced those results showing that the SeV V protein physically interacted with RIG-I and IRF3 as well as MDA5 by IP-Western blotting"
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In Sendai virus-infected, poly(I:C)-stimulated cells, endogenous IRF3 reaches the nucleus only when V is absent, indicating that V retains IRF3 in the cytosol.
"In SeV WT-infected cells, nuclear staining of IRF3 was not observed"
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V inhibits IRF3-driven reporter activation even when the stimulus is a constitutively active IRF3, placing the block at IRF3 itself.
"When the signal was induced by IRF3-5D, the IRF3 activation was restricted in the presence of the V protein but not in the presence of the P/V and Vu proteins."
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Mouse genetics argue that MDA5 is not the sensor responsible for the innate response that V suppresses in vivo; RIG-I is.
"we infected MDA5-knockout mice with V-deficient SeV and found that MDA5 was largely unrelated to the innate immunity that the V protein suppresses in vivo"
Paramyxovirus V Proteins Interact with the RIG-I/TRIM25 Regulatory Complex and Inhibit RIG-I Signaling.
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The Sendai virus V protein co-immunoprecipitates with TRIM25 and with RIG-I, as do the Nipah, measles and PIV5 V proteins.
"Immunoprecipitation against the V5 tag revealed that the V proteins of MeV, NiV, and SeV all coprecipitated with TRIM25, whereas NiV W did not"
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V binding to RIG-I and TRIM25 prevents TRIM25-mediated ubiquitination of RIG-I and the downstream RIG-I interaction with MAVS; this was demonstrated with the Nipah, measles and PIV5 V proteins, not with the Sendai virus protein.
"we show that V interaction with TRIM25 and RIG-I prevents TRIM25-mediated ubiquitination of RIG-I and disrupts downstream RIG-I signaling to the mitochondrial antiviral signaling protein"
Sendai Virus V Protein Inhibits the Secretion of Interleukin-1β by Preventing NLRP3 Inflammasome Assembly.
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V binds host NLRP3 and blocks its self-oligomerization and the NLRP3-dependent oligomerization of ASC that the inflammasome requires.
"we showed that the V protein of SeV inhibits NLRP3 self-oligomerization by interacting with NLRP3 to block the NLRP3-mediated ASC oligomerization required for full activation of the inflammasome"
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NLRP3 is required for the interleukin-1-beta secretion provoked by V-deficient Sendai virus in THP1 macrophages.
"indicating that NLRP3 is required for SeV V"
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Inhibition tracks with NLRP3 binding across V truncations, and the zinc-site point mutant Vcys retains both.
"Wild-type V and Vcys, but not Vn and Vc, inhibited NLRP3 inflammasome-dependent IL-1"