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USP19 suppresses cellular type I interferon signaling by targeting TRAF3 for deubiquitination

To investigate host factors that mediate the immune escape of enterovirus 71 (EV71) in the context of deubiquitinating enzymes. 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 iden...

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Bibliographic Details
Published in:Future microbiology 2017-07, Vol.12 (9), p.767-779
Main Authors: Gu, Zhiwen, Shi, Weifeng, Zhang, Li, Hu, Zhilin, Xu, Chao
Format: Article
Language:English
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Summary:To investigate host factors that mediate the immune escape of enterovirus 71 (EV71) in the context of deubiquitinating enzymes. 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. EV71 infection induces the upregulation of ubiquitin-specific protease 19 ( ) 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. This work suggests that USP19 is a previously unrecognized regulator employed by EV71 to evade host antiviral defenses.
ISSN:1746-0913
1746-0921
DOI:10.2217/fmb-2017-0006