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TRIM14 inhibits hepatitis C virus infection by SPRY domain-dependent targeted degradation of the viral NS5A protein.

Sci Rep. 2016; 
Wang Shanshan,Chen Yongzhi,Li Chunfeng,Wu Yaoxing,Guo Lei,Peng Changwei,Huang Yueping,Cheng Genhong,Qin F Xiao-
Products/Services Used Details Operation
Recombinant Antibody Services Recombinant Human IFN-α , IFN-β , IFN-γ (Peprotech), Monoclonal anti-Flag M2-Peroxidase (Sigma), anti-HA-peroxidase (Roche), Mouse anti-beta actin antibody (Genscript), and rabbit anti-TRIM14 antibody was raised against recombinant human full-length TRIM14 (Aviva Systems Biology), MG132, G418, polybrene and dimethyl sulfoxide (DMSO) were purchased from Sigma. Get A Quote

摘要

Tripartite motif 14 (TRIM14) was reported to function as a mitochondrial signaling adaptor in mediating innate immune responses. However, the involvement of TRIM14 in host defense against viral infection and molecular mechanisms remain unclear. Here, we demonstrated that enforced expression of TRIM14 could potently inhibit the infection and replication of HCV in hepatocytes, whereas TRIM14 knockout cells became more susceptible to HCV infection. Interestingly, further experiments revealed that such anti-HCV activity was independent of activating the NF-κB or interferon pathways but required the C-terminal SPRY domain of no signaling capacity. In searching for mechanisms how TRIM14 exerts its antiviral ... More

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