In:
The EMBO Journal, EMBO, Vol. 41, No. 18 ( 2022-09-15)
Kurzfassung:
image Viruses often subvert host proteins for their amplification, but host subversion of virus proteins to regulate viral proliferation has not been reported in plants. This work shows that a plant‐viral virulence protein is phosphorylated by host kinases, with the phosphorylated form becoming an inhibitor of AGO1‐associated vsiRNAs cleavage and thus enhancing the abundance of antiviral RNAi. The 17K protein of barley yellow dwarf virus (BYDV) is phosphorylated by host GRIK1‐SnRK1 kinases. The phosphorylated 17K (P17K) interacts with host small RNA degrading nuclease 1 (HvSDN1) and Argonaute 1 (HvAGO1), and binds BYDV vsiRNA. P17K inhibits the cleavage of HvAGO1‐associated vsiRNAs by HvSDN1, thus elevating vsiRNA abundance and resulting in enhanced antiviral RNAi. Transgenic expression of a 17K phosphomimetic (17K 5D ), or genome editing of SDN1 , generates stable resistance to BYDV through elevating vsiRNA abundance.
Materialart:
Online-Ressource
ISSN:
0261-4189
,
1460-2075
DOI:
10.15252/embj.2021110521
Sprache:
Englisch
Verlag:
EMBO
Publikationsdatum:
2022
ZDB Id:
1467419-1
ZDB Id:
586044-1
SSG:
12
