文献类型： 外文期刊

作者： Qin, Li ¹ ; Liu, Hongjun ¹ ; Liu, Peilan ¹ ; Jiang, Lu ¹ ; Cheng, Xiaofei ⁴ ; Li, Fangfang ³ ; Shen, Wentao ⁵ ; Qiu, Wenping ⁶ ; Dai, Zhaoji ¹ ; Cui, Hongguang ¹ ;

作者机构： 1.Hainan Univ, Key Lab Green Prevent & Control Trop Dis & Pests, Minist Educ, Haikou 570228, Peoples R China

2.Hainan Univ, Sch Trop Agr & Forestry, Haikou, Peoples R China

3.Chinese Acad Agr Sci, State Key Lab Biol Plant Dis & Insect Pests, Inst Plant Protect, Beijing, Peoples R China

4.Northeast Agr Univ, Coll Plant Protect, Key Lab Germplasm Enhancement Physiol & Ecol Food, Chinese Educ Minist, Harbin, Peoples R China

5.Chinese Acad Trop Agr Sci, Inst Trop Biosci & Biotechnol, Haikou, Peoples R China

6.Missouri State Univ, William H Darr Coll Agr, Ctr Grapevine Biotechnol, Mt Grove, MO USA

期刊名称：PLOS PATHOGENS （ 影响因子：6.7； 五年影响因子：6.7 ）

ISSN： 1553-7366

年卷期： 2024 年 20 卷 3 期

页码：

收录情况： SCI

摘要： Plant viruses must move through plasmodesmata (PD) to complete their life cycles. For viruses in the Potyviridae family (potyvirids), three viral factors (P3N-PIPO, CI, and CP) and few host proteins are known to participate in this event. Nevertheless, not all the proteins engaging in the cell-to-cell movement of potyvirids have been discovered. Here, we found that HCPro2 encoded by areca palm necrotic ring spot virus (ANRSV) assists viral intercellular movement, which could be functionally complemented by its counterpart HCPro from a potyvirus. Affinity purification and mass spectrometry identified several viral factors (including CI and CP) and host proteins that are physically associated with HCPro2. We demonstrated that HCPro2 interacts with both CI and CP in planta in forming PD-localized complexes during viral infection. Further, we screened HCPro2-associating host proteins, and identified a common host protein in Nicotiana benthamiana-Rubisco small subunit (NbRbCS) that mediates the interactions of HCPro2 with CI or CP, and CI with CP. Knockdown of NbRbCS impairs these interactions, and significantly attenuates the intercellular and systemic movement of ANRSV and three other potyvirids (turnip mosaic virus, pepper veinal mottle virus, and telosma mosaic virus). This study indicates that a nucleus-encoded chloroplast-targeted protein is hijacked by potyvirids as the scaffold protein to assemble a complex to facilitate viral movement across cells. Potyviridae is the largest family of RNA viruses in the plant kingdom, consisting of genetically diverse members that adversely affect agriculturally and economically important crops. However, viral and host components in the local movement of potyvirids, an essential step for viruses to spread through the whole plant, are still not fully understood. Thus far, three viral factors (P3N-PIPO, CI and CP) and several host proteins are known to be engaged coordinately in this event. Here, we found that another viral protein, HCPro2, also aids a potyvirid in the intercellular movement. HCPro2 facilitates the virus to move through plasmodesmata (PD), the gate between two plant cells, by forming a complex with CI and CP. More intriguingly, we found that NbRbCS, one of the most abundant proteins in a plant cell, interacts with all the above viral factors in mediating viral movement across plant cells. Reduction of NbRbCS levels greatly impairs the intercellular movement of four tested potyvirids. These data suggest that a common chloroplast protein is co-opted as a pro-viral factor in assembling a complex for viral movement. This finding provides a new insight in our understanding of potyvirids' movement in plants.