ArticleJournal of microbiology, immunology, and infection = Wei mian yu gan ran za zhi2017
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.
Article in Journal of microbiology, immunology, and infection = Wei mian yu gan ran za zhi, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- A global map for introgressed structural variation and selection in humans.Science (New York, N.Y.) · 2026Article
- SARS-CoV-2 Nsp8 suppresses MDA5 antiviral immune responses by impairing TRIM4-mediated K63-linked polyubiquitination.PLoS pathogens · 2023Article
- Methodology-Centered Review of Molecular Modeling, Simulation, and Prediction of SARS-CoV-2.Chemical reviews · 2022Review
- Pathomechanisms, therapeutic targets and potent inhibitors of some beta-coronaviruses from bench-to-bedside.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2021Review
- Phage Display Technique as a Tool for Diagnosis and Antibody Selection for Coronaviruses.Current microbiology · 2021Review
- Application of Bayesian phylogenetic inference modelling for evolutionary genetic analysis and dynamic changes in 2019-nCoV.Briefings in bioinformatics · 2021Article
- Genomic regions associated with microdeletion/microduplication syndromes exhibit extreme diversity of structural variation.Genetics · 2021Article
- Type I and Type III Interferons Restrict SARS-CoV-2 Infection of Human Airway Epithelial Cultures.Journal of virology · 2020Article
- The current landscape of coronavirus-host protein-protein interactions.Journal of translational medicine · 2020Review
- Article
- Human core duplicon gene families: game changers or game players?Briefings in functional genomics · 2019Article
- SARS-Coronavirus Open Reading Frame-3a drives multimodal necrotic cell death.Cell death & disease · 2018Article
- Host Factors in Coronavirus Replication.Current topics in microbiology and immunologyReview
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
background/purposeSevere acute respiratory syndrome coronavirus (SARS-CoV) proteins including ORF6 inhibit Type I interferon (IFN) signaling.
methodsThis 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.
resultsThe 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.
conclusionThe 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.
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