ArticleScientific reports2018
The antiviral protein Viperin suppresses T7 promoter dependent RNA synthesis-possible implications for its antiviral activity.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Discovery of an Antiviral Electron Transfer Process to Create Catalytically Self-Sufficient Viral Restriction Factors.Angewandte Chemie (International ed. in English) · 2026Article
- Nucleotide Immune Signaling in CBASS, Pycsar, Thoeris, and CRISPR Antiphage Defense.Annual review of microbiology · 2024Review
- Chemoenzymatic Synthesis of 3'-Deoxy-3',4'-didehydro-cytidine triphosphate (ddhCTP).ACS bio & med chem Au · 2023Article
- PIK3CA mutation in endometriotic epithelial cells promotes viperin-dependent inflammatory response to insulin.Reproductive biology and endocrinology : RB&E · 2023Article
- Viperin triggers ribosome collision-dependent translation inhibition to restrict viral replication.Molecular cell · 2022Article
- A Review on Transcriptional Responses of Interactions between Insect Vectors and Plant Viruses.Cells · 2022Review
- Structural Insight into the Substrate Scope of Viperin and Viperin-like Enzymes from Three Domains of Life.Biochemistry · 2021Article
- Viperin Reveals Its True Function.Annual review of virology · 2020Review
- Cytosine drives evolution of SARS-CoV-2.Environmental microbiology · 2020Article
- Interactions between Viperin, Vesicle-Associated Membrane Protein A, and Hepatitis C Virus Protein NS5A Modulate Viperin Activity and NS5A Degradation.Biochemistry · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viperin is a multifunctional interferon-inducible broad-spectrum antiviral protein. Viperin belongs to the S-Adenosylmethionine (SAM) superfamily of enzymes known to catalyze a wide variety of radical-mediated reactions. However, the exact mechanism by which viperin exerts its functions is still unclear. Interestingly, for many RNA viruses viperin was shown to inhibit viral RNA accumulation by interacting with different viral non-structural proteins. Here, we show that viperin inhibits RNA synthesis by bacteriophage T7 polymerase in mammalian cells. This inhibition is specific and occurs at the RNA level. Viperin expression significantly reduced T7-mediated cytoplasmic RNA levels. The data showing that viperin inhibits the bacteriophage T7 polymerase supports the conservation of viperin's antiviral activity between species. These results highlight the possibility that viperin might utilize a broader mechanism of inhibition. Accordingly, our results suggest a novel mechanism involving polymerase inhibition and provides a tractable system for future mechanistic studies of viperin.
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