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Loss-of-Function of Two PD-Associated Proteins Confers Resistance to Rice Stripe Virus

文献类型： 外文期刊

作者： Lu, Hong 1 ; Ge, Panpan 1 ; Ma, Yonghuan 1 ; Lin, Feng 3 ; Jing, Dedao 4 ; Zhou, Tong 3 ; Cui, Feng 1 ;

作者机构： 1.Chinese Acad Sci, Inst Zool, State Key Lab Anim Biodivers Conservat & Integrate, Beijing, Peoples R China

2.Univ Chinese Acad Sci, Beijing, Peoples R China

3.Jiangsu Acad Agr Sci, Inst Plant Protect, Key Lab Food Qual & Safety, Nanjing, Peoples R China

4.Zhenjiang Inst Agr Sci Ning Zhen Hilly Dist, Zhenjiang, Peoples R China

关键词： flotillin; importin alpha; PD-associated protein; plasmodesmata; rice; rice stripe virus

期刊名称：MOLECULAR PLANT PATHOLOGY （ 影响因子：4.9； 五年影响因子：5.6 ）

ISSN： 1464-6722

年卷期： 2025 年 26 卷 7 期

页码：

收录情况： SCI

摘要： Plant viruses usually exploit plasmodesmata (PDs) to achieve cellular infection in host plants. Although PD-associated proteins are commonly implicated in the regulation of PD pore size, a few limited cases demonstrate their roles as viral targets suitable for resistance breeding. Here we screened the importin alpha protein family of rice to identify the PD-associated members and explored their effects on the infection of rice stripe virus (RSV), one of the most notorious pathogens threatening rice yields. Both Importin alpha 1b and alpha 4 were found to be localised on the plasma membrane and PD. Only importin alpha 4 knockout mutant rice exhibited resistance to RSV infection while the role of importin alpha 1b in RSV infection was negligible. The absence of importin alpha 4 enhanced callose deposition at PDs, which impeded viral intercellular movement. Flotillin 1 is another PD-associated protein in rice and was previously reported to facilitate RSV infection. When flotillin1 and importin alpha 4 were simultaneously knocked out, the double-knockout mutant exhibited a synergically higher resistance level to RSV not only in the greenhouse but also in natural fields without affecting agronomic traits. This study proposed the potential of the two PD-associated proteins as targets for engineering virus resistance in future.

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