{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRSAD2, commonly known as viperin, is a highly conserved, interferon‐stimulated radical S‐adenosylmethionine (SAM) enzyme that plays a central role in innate antiviral defense. Upon viral infection, viperin is rapidly induced and exerts its antiviral activity by catalyzing the transformation of cytidine triphosphate (CTP) into a modified nucleotide (ddhCTP) that acts as a chain terminator for viral RNA‐dependent RNA polymerases. This enzymatic activity, dependent on an intact [4Fe‐4S] cluster and conserved SAM motifs, underlies its capacity to directly impair the replication of a diverse range of viruses. In addition, fundamental studies have linked viperin’s biochemical function to its ability to alter cellular membranes and interact with critical host enzymes, suggesting that its radical SAM activity is evolutionarily conserved even in prokaryotes as a natural antiviral strategy."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its intrinsic enzymatic activity, viperin exerts antiviral effects by interacting with both viral and host proteins to disrupt key steps in the viral life cycle. It impairs virus assembly, budding, and release by altering the composition and fluidity of cellular membranes, particularly at the endoplasmic reticulum and lipid droplets. For example, viperin can interfere with the activity of farnesyl diphosphate synthase and directly interact with viral nonstructural proteins such as NS5A or NS3 in hepatitis C and flavivirus infections, thereby destabilizing viral replication complexes. These multifaceted interactions also include recruitment of components involved in protein ubiquitination and proteasomal degradation, collectively contributing to a blockade of virus replication and spread."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, viperin has emerged as a pivotal modulator of broader cellular metabolic and signaling pathways which indirectly influence viral infectivity. By downregulating cholesterol and lipid biosynthesis pathways, viperin disrupts lipid raft formation—a feature essential for the budding of many enveloped viruses. It also interfaces with innate immune signaling cascades, modulating cytokine production and ubiquitin-dependent protein degradation to further restrict both viral replication and even intracellular bacterial pathogens. Collectively, these direct and indirect antiviral mechanisms underscore viperin’s importance as an effector of the interferon response and highlight its potential as a target for therapeutic intervention against a wide spectrum of pathogens."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "P S Olofsson, K Jatta, D Wågsäter, et al. 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