Author: Sun, Di; Chen, Shun; Cheng, Anchun; Wang, Mingshu
Title: Roles of the Picornaviral 3C Proteinase in the Viral Life Cycle and Host Cells Document date: 2016_3_17
ID: 07nfb69o_47
Snippet: The 3C pro of another, HAV, has the capability to induce proteolysis of MAVS by the viral 3ABC precursor. The cleavage of this mitochondrially localized adaptor of RIG-I and MDA5 disrupts activation of IRF3 and abolishes type I IFN responses. The protease activities of 3C pro and the transmembrane domain of 3A are both necessary for the proteolysis of MAVS [112, 113] . For another precursor, HAV 3CD protease-polymerase disrupts TLR3 signaling by .....
Document: The 3C pro of another, HAV, has the capability to induce proteolysis of MAVS by the viral 3ABC precursor. The cleavage of this mitochondrially localized adaptor of RIG-I and MDA5 disrupts activation of IRF3 and abolishes type I IFN responses. The protease activities of 3C pro and the transmembrane domain of 3A are both necessary for the proteolysis of MAVS [112, 113] . For another precursor, HAV 3CD protease-polymerase disrupts TLR3 signaling by degrading TRIF (Figure 6 ) and this degradation is not dependent on only the protease activity of 3C pro but also requires the 3D sequence to modulate the substrate specificity of 3C pro [114] . NEMO, a bridging adaptor protein for the activation of NF-κB, is another substrate of HAV 3C pro at the Q304 residue (Table 4 ) [115] . NEMO is also cleaved by FMDV 3C pro at the Gln-383 residue but not by the 3C pro of EV 71 [116] .
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