Author: Yang, Darong; Li, Nan L.; Wei, Dahai; Liu, Baoming; Guo, Fang; Elbahesh, Husni; Zhang, Yunzhi; Zhou, Zhi; Chen, Guo-Yun; Li, Kui
Title: The E3 ligase TRIM56 is a host restriction factor of Zika virus and depends on its RNA-binding activity but not miRNA regulation, for antiviral function Document date: 2019_6_28
ID: 1nr0hggt_61
Snippet: While future studies are needed to define the boundary of the RNA-binding motif(s) within TRIM56, we favor a model in which the structured NHL-like domain mediates the interaction with viral RNA. Lending support to this notion, our previous studies have shown that the integrity of the TRIM56 C-terminal portion is essential for inhibiting viral RNA replication of BVDV, DENV2 and YFV, and that two different C-terminal deletion mutants, Δaa 621-695.....
Document: While future studies are needed to define the boundary of the RNA-binding motif(s) within TRIM56, we favor a model in which the structured NHL-like domain mediates the interaction with viral RNA. Lending support to this notion, our previous studies have shown that the integrity of the TRIM56 C-terminal portion is essential for inhibiting viral RNA replication of BVDV, DENV2 and YFV, and that two different C-terminal deletion mutants, Δaa 621-695 and Δaa 693-750, each lacking a separate portion of the NHL-like domain, invariably lost antiviral activity [24, 25] . Whether TRIM56 binds to these flaviviral RNAs via its C-terminal NHLlike domain to exert the observed antiviral effects, as it does with ZIKV RNA, warrants further investigation.
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