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Poly(C)-binding protein 2 positively regulates interferon downstream signaling.

Host innate immunity protection against pathogen infection is universal in diverse species of invertebrates and vertebrates. Type I interferon (IFN-I) is induced by pathogen infection and secreted from the pathogen-infected host cells, and then binds to IFN-I receptors (IFNAR1 and IFNAR2) on the cell surface. This binding leads to the activation of the receptor-associated Janus-activated kinase 1 (Jak1) and tyrosine kinase 2 (Tyk2). Then the activated kinases phosphorylate the signal transducer and activator of tran-scription proteins 1 and 2 (STAT1 and STAT2). Afterwards, the activated STAT1/2 complex combines with IFN-regulatory factor 9 (IRF9) to form a complex that binds to the IFN-stimulated response elements on cellular DNA, which leads to the expression of the multiple IFN-stimulated genes (ISGs) [1,2]. Due to the importance of JAK-STAT pathway to antiviral immunity, down-regulation of the IFN-I receptors will result in a disastrous damage of an IFN-I antiviral res-ponse. Therefore, maintaining IFNAR1 protein stability is a matter of cardinal importance for the enhancement of the antiviral efficacy of IFN-I.