Key result
EV71 infection upregulates USP19, which suppresses cellular type I interferon signaling by targeting TRAF3 and decreasing its K63-linked ubiquitination to evade host antiviral defenses.
USP19 is a host factor exploited by EV71 to evade antiviral defenses by suppressing type I interferon signaling via TRAF3 deubiquitination.
USP19 upregulation may mediate EV71 immune escape; leaves open its value as antiviral target pending validation.
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.
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Gu et al. (2017) studied Enterovirus 71 (EV71) infection. EV71 infection was evaluated on Cellular antiviral type I interferon signaling and TRAF3 ubiquitination. EV71 infection upregulates USP19, which suppresses cellular type I interferon signaling by targeting TRAF3 and decreasing its K63-linked ubiquitination to evade host antiviral defenses.
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