Rice stripe virus nonstructural protein 3 suppresses plant defence responses mediated by the MEL-SHMT1 module

被引:2
作者
Wang, Kun [1 ]
Fu, Shuai [1 ,2 ]
Wu, Liang [1 ]
Wu, Jianxiang [1 ]
Wang, Yaqin [1 ,4 ]
Xu, Yi [3 ]
Zhou, Xueping [1 ,2 ,4 ]
机构
[1] Zhejiang Univ, Coll Agr & Biotechnol, State Key Lab Rice Biol, Hangzhou, Peoples R China
[2] Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing, Peoples R China
[3] Nanjing Agr Univ, Coll Plant Protect, Dept Plant Pathol, Nanjing, Peoples R China
[4] Zhejiang Univ, Coll Agr & Biotechnol, State Key Lab Rice Biol & Breeding, Hangzhou 310058, Peoples R China
关键词
E3; ligase; NS3; plant defence response; Rice stripe virus; SHMT1; SALICYLIC-ACID; DISEASE; UBIQUITINATION; DEGRADATION; RECEPTORS; IMMUNITY;
D O I
10.1111/mpp.13373
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Our previous study identified an evolutionarily conserved C4HC3-type E3 ligase, named microtubule-associated E3 ligase (MEL), that regulates broad-spectrum plant resistance against viral, fungal and bacterial pathogens in multiple plant species by mediating serine hydroxymethyltransferase (SHMT1) degradation via the 26S proteasome pathway. In the present study, we found that NS3 protein encoded by rice stripe virus could competitively bind to the MEL substrate recognition site, thereby inhibiting MEL interacting with and ubiquitinating SHMT1. This, in turn, leads to the accumulation of SHMT1 and the repression of downstream plant defence responses, including reactive oxygen species accumulation, mitogen-activated protein kinase pathway activation, and the up-regulation of disease-related gene expression. Our findings shed light on the ongoing arms race between pathogens and demonstrate how a plant virus can counteract the plant defence response.
引用
收藏
页码:1359 / 1369
页数:11
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