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http://purl.uniprot.org/citations/26320399http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26320399http://www.w3.org/2000/01/rdf-schema#comment"

Background/purpose

Severe acute respiratory syndrome coronavirus (SARS-CoV) proteins including ORF6 inhibit Type I interferon (IFN) signaling.

Methods

This study identified SARS-CoV ORF6-interacting proteins using the phage displayed human lung cDNA libraries, and examined the association of ORF6-host factor interaction with Type I IFN antagonism. After the fifth round of biopanning with Escherichia coli-synthesized ORF6-His tagged protein, the relative binding affinity of phage clones to ORF6 was determined using direct enzyme-linked immunosorbent assay.

Results

The highest affinity clone to ORF6 displayed the C-terminal domain of NPIPB3 (nuclear pore complex interacting protein family, member B3; also named as phosphatidylinositol-3-kinase-related kinase SMG-1 isoform 1 homolog). The coimmunoprecipitation assay demonstrated the direct binding of ORF6 to the C-terminal domain of NPIPB3 in vitro. Confocal imaging revealed a close colocalization of SARS-CoV ORF6 protein with NPIPB3 in human promonocytes. The dual luciferase reporter assay showed that the C-terminal domain of NPIPB3 attenuated the antagonistic activity of SARS-CoV ORF6 on IFN-β-induced ISRE (IFN stimulated response element)-responsive firefly luciferase activity. In addition, confocal imaging and Western blotting assays revealed that the increases in STAT-1 nuclear translocation and phosphorylation occurred in the transfected cells expressing both genes of ORF6 and NPIPB3, but not in the ORF6-expressing cells in response to IFN-β.

Conclusion

The overexpression of NPIPB3 restored the IFN-β responses in SARS-CoV ORF6 expressing cells, indicating that the interaction of SARS CoV ORF6 and NPIPB3 reduced Type I IFN antagonism by SARS-CoV ORF6."xsd:string
http://purl.uniprot.org/citations/26320399http://purl.org/dc/terms/identifier"doi:10.1016/j.jmii.2015.07.002"xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/author"Wan L."xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/author"Lai C.H."xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/author"Lin Y.J."xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/author"Lee T.Y."xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/author"Huang S.H."xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/author"Lin C.W."xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/name"J Microbiol Immunol Infect"xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/pages"277-285"xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/title"Phage display technique identifies the interaction of severe acute respiratory syndrome coronavirus open reading frame 6 protein with nuclear pore complex interacting protein NPIPB3 in modulating Type I interferon antagonism."xsd:string
http://purl.uniprot.org/citations/26320399http://purl.uniprot.org/core/volume"50"xsd:string
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