Key result
Enterovirus D68 2A protease inhibits antiviral type I interferon responses by cleaving tumor necrosis factor receptor-associated factor 3 (TRAF3).
Why the study?
The pathogenic mechanism of human enterovirus 68 (EV-D68) is not fully understood despite its emergence as a global reemergent pathogen causing severe respiratory tract infections and acute flaccid myelitis.
This is the authors' abstract. We don't add key points for this paper.
Human enterovirus 68 (EV-D68) has received considerable attention recently as a global reemergent pathogen because it causes severe respiratory tract infections and acute flaccid myelitis. The nonstructural protein 2A protease (2Apro) of EV, which functions in cleavage of host proteins, comprises an essential part of the viral immune evasion process. However, the pathogenic mechanism of EV-D68 is not fully understood. Here, we show for the first time that EV-D68 inhibited antiviral type I interferon responses by cleaving tumor necrosis factor receptor-associated factor 3 (TRAF3). Furthermore, we identified the key cleavage site in TRAF3. Our study may suggest a new mechanism by which the 2Aproof EV facilitates subversion of host innate immune responses. These findings increase our understanding of EV-D68 infection and may help identify new antiviral targets against EV-D68.
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EV-D68 evades host innate immunity by using its 2A protease to cleave TRAF3, identifying a potential new antiviral target.
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Kang et al. (2020) studied Enterovirus D68 infection. Enterovirus D68 2A protease (2Apro) was evaluated on Cleavage of tumor necrosis factor receptor-associated factor 3 (TRAF3) and inhibition of antiviral type I interferon responses. Enterovirus D68 2A protease inhibits antiviral type I interferon responses by cleaving tumor necrosis factor receptor-associated factor 3 (TRAF3).
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