{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nOAS1 (2′-5′-oligoadenylate synthetase 1) is a type I interferon–inducible enzyme that plays a central role in the innate antiviral response by sensing cytosolic double‐stranded RNA. Upon binding to viral dsRNA, OAS1 undergoes a conformational change that permits it to catalyze the synthesis of 2′-5′ oligoadenylates from ATP. These oligoadenylates in turn activate RNase L, which degrades viral (and cellular) RNAs to restrict viral replication. Genetic studies have linked OAS1 polymorphisms and splice variants to differential antiviral activity and disease outcomes in infections caused by hepatitis C virus, West Nile virus, SARS‐CoV‐2, and even respiratory syncytial virus, while increased circulating levels of OAS1 are associated with protection from severe COVID-19."}, {"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": "\nStructural and mechanistic investigations have revealed that OAS1 recognizes dsRNA through previously uncharacterized interfaces that prompt extensive conformational rearrangements, thereby organizing its catalytic center for coordinating essential magnesium ions and nucleotide substrates. Sequence‐specific and context‐dependent features of dsRNA, including defined RNA motifs, further modulate the extent of OAS1 activation. In addition, cis‐regulatory studies and expression quantitative trait locus analyses in autoimmune conditions have shown that genetic variants influencing OAS1 splicing—and hence the production of distinct isoforms such as the prenylated p46 variant—are critical determinants of its enzymatic activity and downstream RNase L–mediated responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical antiviral role, aberrant OAS1 activity—whether through hypofunctional alleles that increase host susceptibility to viral infections or through gain‐of‐function mutations that lead to inappropriate, dsRNA‐independent activation of RNase L—has been implicated in a range of pathological conditions. These include autoinflammatory immunodeficiencies (where OAS1 mutations cause excessive RNase L activation and cellular dysfunction), altered immune regulation in macrophages (modulating chemokine and interferon‐stimulated gene expression), and associations with chronic diseases such as type 1 diabetes, multiple sclerosis, and even prostate cancer. Moreover, certain viruses (for example, human cytomegalovirus) have evolved proteins that antagonize OAS1 function, thereby subverting this critical innate immune pathway."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "22", "end_ref": "37"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "S Knapp, L J Yee, A J Frodsham, et al. 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