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. 2020 Sep 4;11:517461. doi: 10.3389/fmicb.2020.517461

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Copyright © 2020 Hu, Zhang and Liu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Role of PTMs in alleviating NS1 antagonism of the host antiviral response. (A) Phosphorylation of NS1 at S42 by PKCα can block NS1 binding to dsRNA, alleviating NS1-induced inhibition of OAS activation and RNA degradation. (B) Phosphorylation of NS1 at T49 leads to decreased interaction with dsRNA, TRIM25, and RIG-I, resulting in defective suppression of IFN production. (C) Phosphorylation of NS1 at T80 reduces the binding affinity between NS1 and RIG-I, preventing NS1 from inhibiting IFN production. (D) Herc5-mediated ISGylation of NS1 K126 and K217 inhibits RNA sequestration, alleviating NS1-induced inhibition of OAS activation and RNA degradation. ISGylation of NS1 K126 and K217 impair the NS1 interaction with PKR, which antagonizes NS1-mediated inhibition of host translation. Ub, ubiquitin and ubiquitination; ISG, ISGylation; PKCα, protein kinase C α; OAS, oligo (A) synthetase; TRIM, tripartite motif; PKR, protein kinase R.