The innate immune system detects viral infection by recognizing various viral components and triggers antiviral responses. Like the toll-like receptor 3 (TLR3), the melanoma differentiation-associated protein 5 (MDA5) recognizes double-stranded (ds) RNA, a molecular pattern associated with viral infection. MDA5, a member of the DEAD/DEAH-box RNA helicase family, consists of an amino-terminal caspase recruitment domain (CARD) and a carboxyl-terminal RNA helicase domain similar to that of the related protein RIG-1. When stimulated by dsRNA, MDA5 recruits the adaptor protein VISA and ultimately causes the activation of IRF-3 and NF-kappaB. MDA5 and RIG-1 recognize different types of dsRNA, with MDA5 recognizing poly (I:C). MDA5-null mice were highly susceptible to infection with picornaviruses, which possess such sequences, demonstrating the importance of MDA5 in innate immunity.

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