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


ABSTRACT: 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.

SUBMITTER: Wang K 

PROVIDER: S-EPMC10576177 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature

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

Wang Kun K   Fu Shuai S   Wu Liang L   Wu Jianxiang J   Wang Yaqin Y   Xu Yi Y   Zhou Xueping X  

Molecular plant pathology 20230705 11


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 inhibitin  ...[more]

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