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USP19 suppresses cellular type I interferon signaling by targeting TRAF3 for deubiquitination
Zhiwen Gu1, Weifeng Shi1, Li Zhang1,2
1Department of Laboratory Medicine, the Third Affiliated Hospital of Soochow University, Changzhou, Jiangsu 213003, PR China.
Aim:
To investigate host factors that mediate the immune escape of enterovirus 71 (EV71) in the context of deubiquitinating enzymes.
Materials & Methods:
Utilize PCR array to screen candidate genes that may be involved in EV71-induced cellular antiviral immune responses, and utilize protein mass spectrometry analysis to identify the functional targets of the candidate regulator.
Results:
EV71 infection induces the upregulation of ubiquitin-specific protease 19 (USP19) gene expression, which negatively regulates cellular antiviral type I interferon signaling. Additionally, we identify that USP19 suppresses cellular type I interferon signaling by targeting tumor necrosis factor receptor-associated factor 3 (TRAF3) molecule and decreasing TRAF3 ubiquitination of K63-linkage.
Conclusion:
This work suggests that USP19 is a previously unrecognized regulator employed by EV71 to evade host antiviral defenses.