期刊
EMBO JOURNAL
卷 41, 期 18, 页码 -出版社
WILEY
DOI: 10.15252/embj.2021110521
关键词
antiviral RNAi; BYDV; small RNA-degrading enzyme; SnRK1; wheat
资金
- Key Science and Technology Program of Henan Province [201300110800]
- Zhongyuan Thousand Talents Program [ZYQR201912168]
- Postdoctoral Science Foundations of China [2020M672231]
- Henan Province [201902032]
This study reveals that hosts can utilize phosphorylated viral proteins to regulate viral proliferation. Phosphorylated 17K protein enhances the abundance of virus-derived small interfering RNAs (vsiRNAs) and strengthens antiviral RNA interference. Additionally, phosphorylated 17K protein interacts with barley small RNA-degrading nuclease 1 (HvSDN1) and impedes its ability to degrade vsiRNAs.
Viruses often usurp host machineries for their amplification, but it remains unclear if hosts may subvert virus proteins to regulate viral proliferation. Here, we show that the 17K protein, an important virulence factor conserved in barley yellow dwarf viruses (BYDVs) and related poleroviruses, is phosphorylated by host GRIK1-SnRK1 kinases, with the phosphorylated 17K (P17K) capable of enhancing the abundance of virus-derived small interfering RNAs (vsiRNAs) and thus antiviral RNAi. Furthermore, P17K interacts with barley small RNA-degrading nuclease 1 (HvSDN1) and impedes HvSDN1-catalyzed vsiRNA degradation. Additionally, P17K weakens the HvSDN1-HvAGO1 interaction, thus hindering HvSDN1 from accessing and degrading HvAGO1-carried vsiRNAs. Importantly, transgenic expression of 17K phosphomimetics (17K(5D)), or genome editing of SDN1, generates stable resistance to BYDV through elevating vsiRNA abundance. These data validate a novel mechanism that enhances antiviral RNAi through host subversion of a viral virulence protein to inhibit SDN1-catalyzed vsiRNA degradation and suggest new ways for engineering BYDV-resistant crops.
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