Upregulation of deubiquitinase UBP16 induced by rice stripe virus infection stabilizes SHMT1 to suppress ROS accumulation and facilitate virus infection in Nicotiana benthamiana
Kun Wang, Yaqin Wang, Shuai Fu, Yuchong Tan, Liang Wu, Yi Xu, Jianxiang Wu, Xueping Zhou
TL;DR
This study shows how a rice stripe virus manipulates a plant's deubiquitination process to weaken its defenses and promote infection.
Contribution
The study reveals a novel mechanism by which RSV uses NbUBP16 to stabilize SHMT1 and suppress ROS accumulation.
Findings
RSV infection upregulates the deubiquitinase NbUBP16 in Nicotiana benthamiana.
NbUBP16 stabilizes SHMT1 by removing polyubiquitination mediated by E3 ligase MEL.
This stabilization suppresses ROS accumulation and promotes RSV infection.
Abstract
Modification of proteins by ubiquitin is a dynamic and reversible process. It is unclear whether rice stripe virus (RSV) can modulate the plant deubiquitination pathway. In this study, we found that RSV infection can specifically upregulate the expression of the deubiquitinase NbUBP16. Further analysis revealed that NbUBP16 stabilizes serine hydroxymethyltrasferase (SHMT1) by binding to NbSHMT1 and removing its polyubiquitination modification mediated by E3 ligase MEL, which inhibits downstream SHMT1-mediated ROS accumulation and thereby facilitates RSV infection. Our findings provide new insights into the molecular arms race between pathogens and plants, demonstrating how a plant virus can undermine plant defenses by hijacking host deubiquitination pathways. The online version contains supplementary material available at 10.1007/s44154-025-00265-2.
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Taxonomy
TopicsUbiquitin and proteasome pathways · Plant Virus Research Studies · Protein Degradation and Inhibitors