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DExH-box helicase 58 (DHX58), also known as LGP2, is an **RNA helicase** and a member of the RIG-I–like receptor (RLR) family, which functions as an intracellular sensor for viral RNA to mediate the **innate antiviral immune response**[1][2][4][5]. Unlike the related RLR proteins RIG-I and MDA5, LGP2 lacks caspase recruitment domains (CARDs) and thus does not signal directly but acts as a regulator, modulating the activity of these other sensors[1]. LGP2/DHX58 can play a dual role—initial reports highlighted its ability to act as a negative regulator by sequestering viral RNA and reducing interferon induction, while subsequent genetic studies revealed that LGP2 is also required for optimal activation of innate immune responses in certain viral infections, indicating a context-dependent modulation of RIG-I/MDA5 signaling[1]. DHX58 is predominantly active in the cytoplasm, exhibits ATP hydrolysis and RNA-binding activity, and is involved in zinc ion binding[1][2][4][5]. This protein is implicated in trimming the balance of the interferon-mediated response, and its dysfunction is connected to impaired antiviral responses and may be linked to immune-related diseases or cancer through its regulatory influence on RNA and immune signaling pathways[1][5][6].
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