The present study proposes the following model of LGP2 in mediating RIG-I signaling: under normal condition, LGP2 invertedly binds to RIG-I (LGP2 helicase domain interacts with RIG-I RD and LGP2 RD binds to RIG-I helicase domain); upon viral infection, cooperative ATP and viral dsRNA binding to RIG-I helicase domain leads to a conformational switch to a closed form with dsRNA, and the CARDs are released to interact with IPS-1 concomitantly (53). This evidence concerns the gene RIGI and viral infectious disease.