数字农科院2.0

Geminivirus βV1- protein activates bZIP17/28mediated UPR signaling to facilitate viral pathogenicity but its activity is attenuated by autophagic degradation in plants

文献类型： 外文期刊

作者： Hu, Tao;Li, Chenyang;Liu, Hui;Su, Chenlu;Wang, Yaqin;Li, Fangfang;Zhou, Xueping

作者机构：

关键词： unfolded protein response;autophagy;geminivirus;beta V1;ER stress;ATG18a

期刊名称： PLANT COMMUNICATIONS

ISSN： 2590-3462

年卷期： 2025 年 6 卷 3 期

页码：

收录情况： SCIE（2025版） ; ; CSCD（2025-2026年度）

摘要： The unfolded protein response (UPR) is a vital cellular pathway that maintains endoplasmic reticulum (ER) homeostasis under conditions of ER stress and is associated with the degradation of misfolded proteins. However, the role of ER-associated degradation in plant-microbe interactions has yet to be explored. In this study, we identified a novel viral protein, (3V1, encoded by the tomato yellow leaf curl betasatellite (TYLCCNB), which is localized to the ER and triggers ER aggregation. Transient expression of (3V1 in Nicotiana benthamiana induces robust ER stress and activates the bZIP17/28 branch of the UPR signaling pathway. The induction of bZIP17/28 by (3V1 is crucial for successful virus infection. Furthermore, we demonstrated that (3V1 is unstable in N. benthamiana mesophyll cells, as it is targeted for autophagic degradation. The autophagy-related protein ATG18a, a key component of autophagosomes, participates in the degradation of (3V1, thereby exerting an anti-viral role. Taken together, our results reveal a novel function of the (3V1 protein and provide the first evidence for involvement of bZIP17/28 and ATG18a in ER-associated autophagic degradation during geminivirus infection. These findings significantly expand our understanding of the arms-race dynamics between plants and viruses.

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