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
The carboxy-terminal acidic domain of Rift Valley Fever virus NSs protein is essential for the formation of filamentous structures but not for the nuclear localization of the protein.
-
NSs expressed alone, without other viral proteins, forms nuclear filaments like those in infected cells
"we expressed NSs in mammalian cells via a recombinant Semliki Forest virus and demonstrated that the protein alone was able to form structures similar to those observed in RVF virus-infected cells"
-
The acidic C-terminal domain is required for filament formation but not for nuclear localisation
"deletion of this acidic carboxy-terminal domain prevents the protein from forming filaments but does not affect its nuclear localization"
-
NSs nuclear residence is unexpected because phlebovirus replication is entirely cytoplasmic
"its role is poorly understood, especially since the replication cycle of all these viruses takes place in the cytoplasm"
TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus.
-
RVFV infection suppresses host RNA synthesis in step with falling TFIIH levels
"infection by RVFV leads to a rapid and drastic suppression of host cellular RNA synthesis that parallels a decrease of the TFIIH transcription factor cellular concentration"
-
NSs binds the p44 subunit of TFIIH and forms nuclear filaments that also contain XPB
"the nonstructural viral NSs protein interacts with the p44 component of TFIIH to form nuclear filamentous structures that also contain XPB subunit of TFIIH"
-
NSs competes with XPD for p44 and sequesters p44 and XPB, preventing TFIIH assembly
"By competing with XPD, the natural partner of p44 within TFIIH, and sequestering p44 and XPB subunits, NSs prevents the assembly of TFIIH subunits"
NSs protein of Rift Valley fever virus blocks interferon production by inhibiting host gene transcription.
-
NSs alone is sufficient to block interferon-beta gene expression transcriptionally
"we demonstrate that NSs is sufficient to block IFN-beta gene expression at the transcriptional level"
-
Anti-interferon activity requires nuclear NSs; mutants that stay cytoplasmic lose it
"In contrast, mutant forms of NSs that had lost their IFN-inhibiting activity remained in the cytoplasm, indicating that nuclear localization plays a role"
-
IRF-3, NF-kappaB and AP-1 are activated normally in the presence of NSs, so the block is not on interferon-specific transcription factors
"In the presence of NSs, IRF-3 was still activated and moved to the nucleus. Likewise, NF-kappaB and AP-1 were activated normally, as shown in electrophoretic mobility shift assays"
-
NSs inhibits a constitutive promoter, consistent with a general TFIIH-based transcription block
"NSs was found to inhibit transcriptional activity of a constitutive promoter, in agreement with recent findings showing that NSs targets the basal cellular transcription factor TFIIH"
-
The authors conclude the block is on interferon gene expression, not on interferon-specific signalling
"NSs, unlike other viral IFN antagonists, does not inhibit IFN-specific transcription factors but blocks IFN gene expression at a subsequent step"
Rescue of infectious rift valley fever virus entirely from cDNA, analysis of virus lacking the NSs gene, and expression of a foreign gene.
-
Viruses lacking part or all of the NSs open reading frame are viable and replicate efficiently in interferon-incompetent cells
"Mutants of MP-12 partially or completely lacking the NSs open reading frame were viable. These NSs deletion mutants replicated efficiently in Vero and 293 cells, but not in MRC-5 cells"
-
Interferon-beta mRNA accumulates after infection with NSs-deletion mutants but not with the parental virus
"accumulation of beta interferon mRNA occurred after infection by these NSs deletion mutants, but not after infection by MP-12"
-
NSs is required for shutoff of host protein synthesis
"The NSs deletion mutants formed larger plaques than MP-12 did in Vero E6 cells and failed to shut off host protein synthesis in Vero cells"
-
Expressing NSs from a plasmid blocked rescue of infectious virus, the opposite of a replication requirement
"whereas NSs protein expression abolished virus rescue"
Inhibition of interferon regulatory factor 3 activation by paramyxovirus V protein.
Virulence factor NSs of rift valley fever virus recruits the F-box protein FBXO3 to degrade subunit p62 of general transcription factor TFIIH.
-
FBXO3, a subunit of E3 ubiquitin ligases, is a host interactor of NSs
"we identified a subunit of E3 ubiquitin ligases, F-box protein FBXO3, as a host cell interactor of NSs"
-
Depleting FBXO3 rescues p62 and raises interferon transcription tenfold
"Small interfering RNA (siRNA)-mediated depletion of FBXO3 rescued p62 protein levels in RVFV-infected cells and elevated IFN transcription by 1 order of magnitude"
-
SKP1 knockdown also protects p62, implicating an SCF-type ligase
"siRNA knockdown of Skp1 also protected p62 from degradation, suggesting involvement in NSs action"
-
Cullin 1, cullin 7 and Rbx1 knockdowns did not rescue p62, so the ligase composition is atypical
"However, knockdown of cullin 1, cullin 7, or Rbx1 could not rescue p62 degradation by NSs"
-
NSs removes specifically the nuclear pool of full-length FBXO3, consistent with acting in the nucleus
"NSs exclusively removes the nuclear pool of full-length FBXO3, likely due to consumption during the degradation process"
-
NSs blocks transcriptional upregulation of type I interferons and destroys TFIIH p62 via the ubiquitin-proteasome pathway
"RVFV NSs blocks transcriptional upregulation of antiviral type I interferons (IFN) and destroys the general transcription factor TFIIH subunit p62 via the ubiquitin/proteasome pathway"
A ΩXaV motif in the Rift Valley fever virus NSs protein is essential for degrading p62, forming nuclear filaments and virulence.
-
Nuclear filament formation depends on the NSs-TFIIH interaction and is central to virulence
"A key component of RVFV virulence is its ability to form nuclear filaments through interactions between the viral nonstructural protein NSs and the host general transcription factor TFIIH"
-
A OmegaXaV motif in NSs binds the p62 subunit of TFIIH, mimicking host NER and transcription factors
"we identify an interaction between a ΩXaV motif in NSs and the p62 subunit of TFIIH"
-
The motif is required for both filament formation and p62 degradation in infected cells
"Functional studies in RVFV-infected cells show that the ΩXaV motif is required for both nuclear filament formation and degradation of p62"
-
The motif is absent from the NSs proteins of other bunyaviruses, matching the RVFV-specific filament phenotype
"the motif is absent in the NSs proteins of other Bunyaviridae-family viruses"
The NSs Protein Encoded by the Virulent Strain of Rift Valley Fever Virus Targets the Expression of Abl2 and the Actin Cytoskeleton of the Host, Affecting Cell Mobility, Cell Shape, and Cell-Cell Adhesion.
-
NSs prevents the antiviral upregulation of Abl2, a major regulator of the actin cytoskeleton
"NSs expression prevented the upregulation of Abl2 (a major regulator of the actin cytoskeleton) expression otherwise induced by avirulent infections and identified here as part of the antiviral response"
-
NSs expression reduces lamellipodia and cell spreading and dissolves adherens junctions in hepatocytes
"strong changes in cell morphology in nonmigrating hepatocytes, with reduction of lamellipodia, cell spreading, and dissolution of adherens junctions"
-
The comparison used NSs-expressing ZH548 and MP12 against the non-expressing ZH548 delta-NSs strain, plus ectopic NSs expression
"while conducting infections with the NSs-expressing virulent (ZH548) and attenuated (MP12) strains of RVFV and the non-NSs-expressing avirulent (ZH548ΔNSs) strain, as well as after the ectopic expression of NSs"
Identification of a major non-structural protein in the nuclei of Rift Valley fever virus-infected cells.
-
A 34-kDa nonstructural protein is present in nuclei of RVFV-infected Vero cells
"A non-structural protein of mol. wt. 34 X 10(3) was demonstrated in the nuclei of Rift Valley fever virus-infected Vero cells"
-
The nuclear protein corresponds to the virus-induced antigen seen in intranuclear inclusions by immunofluorescence
"The protein appears to correspond to the virus-induced antigen demonstrated by indirect immunofluorescence in intranuclear inclusions"
UniProtKB/Swiss-Prot entry P21698 (NSS_RVFVZ), Non-structural protein S
-
NSs escapes host innate immunity by degrading PKR and inhibiting host transcription
"Plays a role in the escape of host innate immune response by"
-
The cytoplasmic pool of NSs uses FBXW11 to degrade PKR
"Cytoplasmic NSs interacts with host FBXW11 to degrade PKR"
-
The nuclear pool of NSs uses FBXO3 and SKP1 to target TFIIH subunit GTF2H1 for proteasomal degradation
"nuclear pool binds to host FBXO3 to target TFIIH subunit GTF2H1 for"
-
NSs forms nuclear amyloid-like filaments about 12 nm wide that may sequester its binding partners
"(PubMed:24403578). Forms nuclear amyloid-like filaments of about 12 nm"
-
NSs is found in both the host nucleus and the host cytoplasm
"SUBCELLULAR LOCATION: Host nucleus"
-
The host cytoplasm location is attributed to PubMed:25918396
"cytoplasm {ECO:0000269|PubMed:25918396}"
-
NSs affects cell morphology and motility, reducing lamellipodia and dissolving adherens junctions
"motility, reduction of lamellipodia, cell spreading, and dissolution of"
-
NSs belongs to the phlebovirus NS-S protein family
"SIMILARITY: Belongs to the phlebovirus NS-S protein family."
Curation notes for RVFV NSs, including the CACAO row-by-row assessment
-
Deep research was unavailable for this review and the literature was assembled by hand from cached publications, UniProt, PMC and QuickGO
"Deep research was unavailable for this review."
-
The GONUTS wiki could not be consulted because the site is offline and no Internet Archive snapshot exists
"both return "This site is temporarily offline while we perform"