ArticleThe Journal of biological chemistry2016
Does Viperin Function as a Radical S-Adenosyl-l-methionine-dependent Enzyme in Regulating Farnesylpyrophosphate Synthase Expression and Activity?
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- Structural insights from active site variants and β-8 loop interactions in viperin-like enzymes.Structure (London, England : 1993) · 2025Article
- Mitochondria function in cytoplasmic FeS protein biogenesis.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Purification of the full-length, membrane-associated form of the antiviral enzyme viperin utilizing nanodiscs.Scientific reports · 2022Article
- Structural Insight into the Substrate Scope of Viperin and Viperin-like Enzymes from Three Domains of Life.Biochemistry · 2021Article
- The Antiviral Enzyme, Viperin, Activates Protein Ubiquitination by the E3 Ubiquitin Ligase, TRAF6.Journal of the American Chemical Society · 2021Article
- Review
- Viperin Reveals Its True Function.Annual review of virology · 2020Review
- Proposed Neuroimmune Roles of Dimethyl Fumarate, Bupropion,Brain sciences · 2020Review
- Viperin: An ancient radical SAM enzyme finds its place in modern cellular metabolism and innate immunity.The Journal of biological chemistry · 2020Review
- Targeting viperin to the mitochondrion inhibits the thiolase activity of the trifunctional enzyme complex.The Journal of biological chemistry · 2020Article
- Interactions between Viperin, Vesicle-Associated Membrane Protein A, and Hepatitis C Virus Protein NS5A Modulate Viperin Activity and NS5A Degradation.Biochemistry · 2020Article
- Structural Basis of the Substrate Selectivity of Viperin.Biochemistry · 2020Article
- Viperin interacts with the kinase IRAK1 and the E3 ubiquitin ligase TRAF6, coupling innate immune signaling to antiviral ribonucleotide synthesis.The Journal of biological chemistry · 2019Article
- Article
- Reconstitution and substrate specificity for isopentenyl pyrophosphate of the antiviral radical SAM enzyme viperin.The Journal of biological chemistry · 2018Article
- Human Viperin Causes Radical SAM-Dependent Elongation of Escherichia coli, Hinting at Its Physiological Role.Biochemistry · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Viperin is an endoplasmic reticulum-associated antiviral responsive protein that is highly up-regulated in eukaryotic cells upon viral infection through both interferon-dependent and independent pathways. Viperin is predicted to be a radical S-adenosyl-l-methionine (SAM) enzyme, but it is unknown whether viperin actually exploits radical SAM chemistry to exert its antiviral activity. We have investigated the interaction of viperin with its most firmly established cellular target, farnesyl pyrophosphate synthase (FPPS). Numerous enveloped viruses utilize cholesterol-rich lipid rafts to bud from the host cell membrane, and it is thought that by inhibiting FPPS activity (and therefore cholesterol synthesis), viperin retards viral budding from infected cells. We demonstrate that, consistent with this hypothesis, overexpression of viperin in human embryonic kidney cells reduces the intracellular rate of accumulation of FPPS but does not inhibit or inactivate FPPS. The endoplasmic reticulum-localizing, N-terminal amphipathic helix of viperin is specifically required for viperin to reduce cellular FPPS levels. However, although viperin reductively cleaves SAM to form 5'-deoxyadenosine in a slow, uncoupled reaction characteristic of radical SAM enzymes, this cleavage reaction is independent of FPPS. Furthermore, mutation of key cysteinyl residues ligating the catalytic [Fe
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