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学者姓名：贾东升
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Abstract ：
Insects transmit diverse arthropod-borne viruses. However, it remains largely unknown whether insect innate immune pathways regulate the expression of antiviral factors to mediate the degradation of viral capsids. Here, we discover that transcription factor Dorsal in leafhopper Toll immune pathway binds to the promoter of vertebrate homolog myxovirus resistance-like (MxL) protein to activate its transcription. MxL associates with two different viral particles, promoting ubiquitinated degradation of viral capsids via E3 ubiquitin ligase SIAH1. Notably, MxL forms biomolecular condensates to recruit capsid protein P8 of a destructive rice reovirus and SIAH1. The disordered N-terminal region of MxL is essential for condensate formation. The Arg residue at position 159 of MxL is essential for MxL-P8 interaction and P8 recruitment into condensates. Viral nonstructural protein Pns11 interacts with Dorsal, effectively blocking its nuclear translocation and attenuating antiviral MxL1 expression. Our finding represents the first evidence that MxLs in invertebrates possess broad-spectrum antiviral functions.
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| GB/T 7714 | Du, Yu , Li, You , Xiao, Yuqing et al. Insect antiviral Mx-like protein forms biomolecular condensates to promote viral capsid ubiquitinated degradation [J]. | CELL REPORTS , 2025 , 44 (8) . |
| MLA | Du, Yu et al. "Insect antiviral Mx-like protein forms biomolecular condensates to promote viral capsid ubiquitinated degradation" . | CELL REPORTS 44 . 8 (2025) . |
| APA | Du, Yu , Li, You , Xiao, Yuqing , Jia, Dongsheng , Wei, Taiyun . Insect antiviral Mx-like protein forms biomolecular condensates to promote viral capsid ubiquitinated degradation . | CELL REPORTS , 2025 , 44 (8) . |
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Rice planthoppers are the most destructive pests of rice production and the vectors of rice viruses. Fenmezoditiaz as a novel mesoionic insecticide is used for rice planthopper management by targeting the insect's neural nicotinic acetylcholine receptor. This study aimed to evaluate the effects of fenmezoditiaz on the acquisition, propagation, and transmission of southern rice black-streaked dwarf virus (SRBSDV) by the white-backed planthopper, Sogatella furcifera (Hemiptera: Delphacida). The results revealed that sublethal concentrations of fenmezoditiaz significantly impaired SRBSDV acquisition and viral replication in S. furcifera. Fenmezoditiaz-treated viruliferous S. furcifera exhibited a lower transmission efficiency of SRBSDV to un-infected rice seedlings. Electrical penetration graph (EPG) recordings revealed prolonged non-probing (NP), salivary secretion (N2/N3), and xylem feeding (N5) durations, alongside shortened phloem contact behavior (N4a/N4b), of fenmezoditiaz-treated individuals, indicating disrupted feeding behaviors, which are critical for reducing viral infection. By reducing viral titers and interfering with phloem ingestion, fenmezoditiaz significantly suppresses SRBSDV transmission. These findings revealed fenmezoditiaz's dual role in pest control and viral transmission blockage, providing a foundation for incorporation into integrated management of vector-borne plant viruses.
Keyword ：
electrical penetration graph electrical penetration graph feeding behaviors feeding behaviors fenmezoditiaz fenmezoditiaz Sogatella furcifera Sogatella furcifera viral transmission viral transmission
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| GB/T 7714 | Chen, Yuting , Mao, Lixin , Ding, Xiulan et al. Fenmezoditiaz Inhibited the Acquisition and Transmission of Southern Rice Black-Streaked Dwarf Virus by Sogatella furcifera [J]. | INSECTS , 2025 , 16 (9) . |
| MLA | Chen, Yuting et al. "Fenmezoditiaz Inhibited the Acquisition and Transmission of Southern Rice Black-Streaked Dwarf Virus by Sogatella furcifera" . | INSECTS 16 . 9 (2025) . |
| APA | Chen, Yuting , Mao, Lixin , Ding, Xiulan , Liu, Hengchien , Vyas, Devendra J. , Jia, Dongsheng . Fenmezoditiaz Inhibited the Acquisition and Transmission of Southern Rice Black-Streaked Dwarf Virus by Sogatella furcifera . | INSECTS , 2025 , 16 (9) . |
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Insect Janus kinase/signal transducer and activator of transcription (JAK/STAT) pathway plays a crucial role in antiviral defense, yet how arboviruses activate this pathway remains unclear. Here, we reveal that outer capsid protein of a double-stranded RNA (dsRNA) arbovirus (rice gall dwarf virus, RGDV) directly binds the Dome receptor's extracellular domain, triggering receptor dimerization and JAK/STAT activation. Structural and mutational analyses pinpoint cysteine 743 in Dome as essential for viral recognition, establishing Dome as the first identified viral pattern recognition receptor (PRR) in insects capable of initiating JAK/ STAT signaling, a pathway previously thought to be exclusively cytokine dependent. Furthermore, we identify viperin as a transcriptional factor STAT-regulated antiviral effector with broad-spectrum activity against multiple rice viruses. Intriguingly, RGDV's nonstructural protein Pns11 competitively binds STAT, blocking its phosphorylation by JAK and nuclear translocation, thereby suppressing viperin expression. These findings elucidate how leafhopper Dome functions as a viral PRR and how arboviruses antagonize Dome-JAK-STAT signaling to promote persistent viral infection.
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| GB/T 7714 | Chen, Siyu , Tang, Yupeng , Zhang, Chunyu et al. Insect dome receptor directly recognizes viral envelopes to activate JAK/STAT signaling and induce conserved antiviral viperin expression [J]. | CELL REPORTS , 2025 , 44 (8) . |
| MLA | Chen, Siyu et al. "Insect dome receptor directly recognizes viral envelopes to activate JAK/STAT signaling and induce conserved antiviral viperin expression" . | CELL REPORTS 44 . 8 (2025) . |
| APA | Chen, Siyu , Tang, Yupeng , Zhang, Chunyu , Li, You , Jia, Dongsheng , Wei, Taiyun . Insect dome receptor directly recognizes viral envelopes to activate JAK/STAT signaling and induce conserved antiviral viperin expression . | CELL REPORTS , 2025 , 44 (8) . |
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Janus kinase/signal transducer and activator of transcription (JAK/STAT) immune response traditionally requires cytokine binding to receptors for activation; however, it remains unclear whether cytokine receptors function as direct pattern recognition receptors (PRRs) that recognise viral envelopes. In this study, we demonstrate that cytokine receptor Domeless (Dome) in leafhopper Recilia dorsalis directly recognises glycoprotein (G) of an important rice rhabdovirus. This binding induces Dome dimerisation, which initiates JAK/STAT pathway and leads to STAT-dependent expression of antiviral immune effector in R. dorsalis (RdIE1). RdIE1 suppresses viral replication by inhibiting the RNA-binding activity of viral large polymerase (L). Dome residue T659 is essential for G recognition and L residues E774 and D775 are required for RdIE1 target. Notably, virus-encoded phosphoprotein competitively inhibits the phosphorylation of STAT by casein kinase II (CK2 beta), thereby abrogating STAT-dependent transactivation of target genes. Our findings redefine Dome as a viral sensor and reveal a biphasic strategy that balances antiviral immunity with persistent viral infection in insect vectors.
Keyword ：
antiviral immune effector antiviral immune effector JAK/STAT pathway JAK/STAT pathway pathogens pathogens persistent viral infection persistent viral infection rhabdovirus rhabdovirus signalling signalling
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| GB/T 7714 | Yu, Tingting , Li, You , Xu, Mengjia et al. Rhabdovirus Glycoprotein Triggers Janus Kinase/Signal Transducer and Activator of Transcription Antiviral Immunity via Direct Recognition by Insect Dome Receptor [J]. | PLANT CELL AND ENVIRONMENT , 2025 , 49 (1) : 94-110 . |
| MLA | Yu, Tingting et al. "Rhabdovirus Glycoprotein Triggers Janus Kinase/Signal Transducer and Activator of Transcription Antiviral Immunity via Direct Recognition by Insect Dome Receptor" . | PLANT CELL AND ENVIRONMENT 49 . 1 (2025) : 94-110 . |
| APA | Yu, Tingting , Li, You , Xu, Mengjia , Wan, Zhihao , Jia, Dongsheng , Wei, Taiyun . Rhabdovirus Glycoprotein Triggers Janus Kinase/Signal Transducer and Activator of Transcription Antiviral Immunity via Direct Recognition by Insect Dome Receptor . | PLANT CELL AND ENVIRONMENT , 2025 , 49 (1) , 94-110 . |
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【目的】水稻矮缩病毒（rice dwarf virus,RDV）引起的水稻矮缩病是危害中国南方水稻生产的重要病害。结合前人的研究基础，利用分子生物学等手段，解析肽聚糖识别蛋白6(PGRP6)参与调控媒介昆虫黑尾叶蝉（Nephotettix cincticeps）体内共生菌携带RDV经卵垂直传播的机制，为水稻病毒病的生物防治提供理论依据。【方法】利用酵母双杂交技术筛选与经卵传播相关蛋白（prp、Nasuia porin、P8）均互作的PGRP，并通过GST pull-down进一步验证其互作关系；利用实时荧光定量PCR技术测定相关基因在无毒和带毒虫体内的表达差异，并分析干扰PGRP6、prp后对共生菌增殖的影响，同时通过Western blot检测对昆虫体内共生菌膜蛋白积累的影响；分析抑制PGRP6表达对叶蝉存活率、子代带毒率、带毒子代的病毒核酸水平的影响，并利用荧光原位杂交（FISH）和免疫荧光标记观察叶蝉卵巢内prp、PGRP6、Nasuia及RDV的分布情况；通过抑菌圈和肽聚糖降解实验验证PGRP6的功能。【结果】黑尾叶蝉的PGRP6与prp、Nasuia porin、P8均存在互作；PGRP6和prp在RDV侵染的黑尾叶蝉中的表达量均显著升高；抑制PGRP6表达可促进共生菌Nasuia和Sulcia的增殖，而抑制prp降低了共生菌的增殖，其功能与PGRP6相反，当两者同时被干扰后对共生菌的增殖无显著影响；ds PGRP6处理导致黑尾叶蝉存活率显著降低，子代带毒率增加，子代昆虫体内的病毒量明显高于对照组；免疫荧光标记发现PGRP6与prp、Nasuia、RDV均在卵巢组织中分布并发生共定位，prp和Nasuia是包裹的位置关系；PGPR6存在抑菌功能，可发挥抑制共生菌增殖的作用。【结论】PGRP6通过抑制黑尾叶蝉体内共生菌的增殖维持卵巢组织内的稳态，其与prp的功能相拮抗，其既确保了黑尾叶蝉的生命活力，又调控了共生菌携带RDV的垂直传播。
Keyword ：
共生菌 共生菌 卵巢 卵巢 富脯氨酸蛋白 富脯氨酸蛋白 抑菌 抑菌 水稻矮缩病毒 水稻矮缩病毒 经卵传播 经卵传播 肽聚糖识别蛋白 肽聚糖识别蛋白 黑尾叶蝉 黑尾叶蝉
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| GB/T 7714 | 徐元元 , 贾东升 , 宾羽 et al. 黑尾叶蝉PGRP6负调控共生菌抑制水稻矮缩病毒的经卵传播 [J]. | 中国农业科学 , 2025 , 58 (05) : 907-917 . |
| MLA | 徐元元 et al. "黑尾叶蝉PGRP6负调控共生菌抑制水稻矮缩病毒的经卵传播" . | 中国农业科学 58 . 05 (2025) : 907-917 . |
| APA | 徐元元 , 贾东升 , 宾羽 , 魏太云 . 黑尾叶蝉PGRP6负调控共生菌抑制水稻矮缩病毒的经卵传播 . | 中国农业科学 , 2025 , 58 (05) , 907-917 . |
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In the field, 80% of plant viruses are transmitted by insect vectors. When ingested by a sap-sucking insect such as Recilia dorsalis, persistently transmitted viruses such as rice stripe mosaic virus (RSMV) infect the gut epithelium and eventually pass to the salivary glands where they will be transmitted to the next rice (Oryza sativa) plant. To efficiently exploit insect vectors for transmission, plant viruses must overcome various immune mechanisms within the vectors, including autophagy. However, understanding how plant viruses overcome insect autophagic defenses remains limited. In this study, we provide evidence that infection with RSMV triggers an autophagic antiviral response in leafhopper cells. In this response, the G protein of RSMV binds to a leafhopper AMP-activated protein kinase (AMPK), leading to enhanced phosphorylation of Beclin-1 (BECN1), thereby inducing autophagy. Knockdown of AMPK and genes encoding members of the phosphoinositide 3-kinase (PI3K) complex composed of the autophagy-related protein 14 (ATG14), BECN1, and vacuolar protein sorting 34 (VPS34) facilitated viral infection in leafhoppers. To suppress leafhopper-induced autophagy, RSMV M protein specifically interacts with ATG14, resulting in the disintegration of PI3K complexes. This leads to reduced phosphatidylinositol-3-phosphate content and thus inhibits the G-protein- induced autophagy. Our study sheds light on the mechanism by which this rice virus evades insect autophagy antiviral defenses.
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| GB/T 7714 | Zhang, Ruonan , Wang, Tengfei , Cheng, Yu et al. Rice stripe mosaic virus M protein antagonizes G-protein-induced antiviral autophagy in insect vectors [J]. | PLOS PATHOGENS , 2025 , 21 (4) . |
| MLA | Zhang, Ruonan et al. "Rice stripe mosaic virus M protein antagonizes G-protein-induced antiviral autophagy in insect vectors" . | PLOS PATHOGENS 21 . 4 (2025) . |
| APA | Zhang, Ruonan , Wang, Tengfei , Cheng, Yu , Qiu, Jiaxin , Jia, Dongsheng , Chen, Hongyan et al. Rice stripe mosaic virus M protein antagonizes G-protein-induced antiviral autophagy in insect vectors . | PLOS PATHOGENS , 2025 , 21 (4) . |
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Many devastating plant viruses are transmitted by insect vectors among plant hosts in a persistent-propagative manner. Pelota (Pelo) is an evolutionarily conserved protein involved in the mRNA surveillance system. In this study, it was found that the accumulation of Pelo proteins are slightly decreased during the propagation of the fijivirus southern rice black-streaked dwarf virus (SRBSDV) in rice and transmission vector planthopper (Sogatella furcifera). The tubular protein P7-1 encoded by SRBSDV interacted with Pelo of rice or planthopper vector. Overexpression or knockdown of Pelo expression inhibits the formation of P7-1 tubules in insect cells, further exerting antiviral activity. Furthermore, overexpression or knockout of Pelo expression in transgenic rice plants also inhibits the effective propagation of SRBSDV as well as two other rice viruses of different families. The slight reduction of Pelo accumulation during SRBSDV propagation in rice and insect vectors would avoid Pelo-mediated excessive inhibition of P7-1 tubule formation, ensuring effective virus propagation. Our findings provide insights into how the up- or down-regulated expression of Pelo in rice hosts and insect vectors elevate their resistance to rice viruses.
Keyword ：
mRNA surveillance system mRNA surveillance system Pelo Pelo Resistance Resistance Rice virus Rice virus
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| GB/T 7714 | Sun, Xinyan , Guan, Heran , Wei, Taiyun et al. The mRNA surveillance factor Pelo restricts rice virus propagation in insect vectors and host plants [J]. | PHYTOPATHOLOGY RESEARCH , 2024 , 6 (1) . |
| MLA | Sun, Xinyan et al. "The mRNA surveillance factor Pelo restricts rice virus propagation in insect vectors and host plants" . | PHYTOPATHOLOGY RESEARCH 6 . 1 (2024) . |
| APA | Sun, Xinyan , Guan, Heran , Wei, Taiyun , Jia, Dongsheng . The mRNA surveillance factor Pelo restricts rice virus propagation in insect vectors and host plants . | PHYTOPATHOLOGY RESEARCH , 2024 , 6 (1) . |
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Many plant arboviruses are persistently transmitted by piercing-sucking insect vectors. However, it remains largely unknown how conserved insect Toll immune response exerts antiviral activity and how plant viruses antagonize it to facilitate persistent viral transmission. Here, we discover that southern rice black-streaked dwarf virus (SRBSDV), a devastating planthopper-transmitted rice reovirus, activates the upstream Toll receptors expression but suppresses the downstream MyD88-Dorsal-defensin cascade, resulting in the attenuation of insect Toll immune response. Toll pathway-induced the small antibacterial peptide defensin directly interacts with viral major outer capsid protein P10 and thus binds to viral particles, finally blocking effective viral infection in planthopper vector. Furthermore, viral tubular protein P7-1 directly interacts with and promotes RING E3 ubiquitin ligase-mediated ubiquitinated degradation of Toll pathway adaptor protein MyD88 through the 26 proteasome pathway, finally suppressing antiviral defensin production. This virus-mediated attenuation of Toll antiviral immune response to express antiviral defensin ensures persistent virus infection without causing evident fitness costs for the insects. E3 ubiquitin ligase also is directly involved in the assembly of virus-induced tubules constructed by P7-1 to facilitate viral spread in planthopper vector, thereby acting as a pro-viral factor. Together, we uncover a previously unknown mechanism used by plant arboviruses to suppress Toll immune response through the ubiquitinated degradation of the conserved adaptor protein MyD88, thereby facilitating the coexistence of arboviruses with their vectors in nature. Many devastating plant viral pathogens are persistently transmitted by arthropod insects without causing evident insect fitness costs. However, how Toll pathway plays an antiviral role and how viruses antagonize Toll antiviral immune response are still poorly understood. Here, we report that the planthopper defensin, a type of antibacterial peptide induced by Toll pathway, directly binds to viral particles of an important rice reovirus, thus exerting antiviral activity. However, the virus-encoded protein promotes the ubiquitinated degradation of the conserved Toll pathway adaptor protein MyD88, finally suppressing defensin production. Such process finally ensures persistent virus transmission by insect vectors. Our findings provide insights into how viruses have evolved the novel strategies to evade and even exploit insect Toll antiviral immune response to facilitate persistent viral transmission.
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| GB/T 7714 | Jia, Dongsheng , Luo, Guozhong , Guan, Heran et al. Arboviruses antagonize insect Toll antiviral immune signaling to facilitate the coexistence of viruses with their vectors [J]. | PLOS PATHOGENS , 2024 , 20 (6) . |
| MLA | Jia, Dongsheng et al. "Arboviruses antagonize insect Toll antiviral immune signaling to facilitate the coexistence of viruses with their vectors" . | PLOS PATHOGENS 20 . 6 (2024) . |
| APA | Jia, Dongsheng , Luo, Guozhong , Guan, Heran , Yu, Tingting , Sun, Xinyan , Du, Yu et al. Arboviruses antagonize insect Toll antiviral immune signaling to facilitate the coexistence of viruses with their vectors . | PLOS PATHOGENS , 2024 , 20 (6) . |
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Catalase (CAT) is the main reactive oxygen species (ROS)-scavenging enzyme in plants and insects. However, it remains elusive whether and how insect saliva CAT suppresses ROS-mediated plant defense, thereby promoting initial virus transmission by insect vectors. Here, we investigated how leafhopper Recilia dorsalis catalase (RdCAT) was secreted from insect salivary glands into rice phloem, and how it was perceived by rice chaperone NO CATALASE ACTIVITY1 (OsNCA1) to scavenge excessive H2O2 during insect-to-plant virus transmission. We found that the interaction of OsNCA1 with RdCAT activated its enzymatic activity to decompose H2O2 in rice plants during leafhopper feeding. However, initial insect feeding did not significantly change rice CATs transcripts. Knockout of OsNCA1 in transgenic lines decreased leafhopper feeding-activated CAT activity and caused higher H2O2 accumulation. A devastating rice reovirus activated RdCAT expression and promoted the cosecretion of virions and RdCAT into leafhopper salivary cavities and ultimately into the phloem. Virus-mediated increase of RdCAT secretion suppressed excessive H2O2, thereby promoting host attractiveness to insect vectors and initial virus transmission. Our findings provide insights into how insect saliva CAT is secreted and perceived by plant chaperones to suppress the early H2O2 burst during insect feeding, thereby facilitating viral transmission.
Keyword ：
catalase catalase H2O2 H2O2 leafhopper leafhopper rice rice saliva proteins saliva proteins viral transmission viral transmission
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| GB/T 7714 | Zhang, Hongxiang , Chi, Yunhua , Chen, Siyu et al. Scavenging H2O2 of plant host by saliva catalase of leafhopper vector benefits viral transmission [J]. | NEW PHYTOLOGIST , 2024 , 243 (6) : 2368-2384 . |
| MLA | Zhang, Hongxiang et al. "Scavenging H2O2 of plant host by saliva catalase of leafhopper vector benefits viral transmission" . | NEW PHYTOLOGIST 243 . 6 (2024) : 2368-2384 . |
| APA | Zhang, Hongxiang , Chi, Yunhua , Chen, Siyu , Lv, Xinwei , Jia, Dongsheng , Chen, Qian et al. Scavenging H2O2 of plant host by saliva catalase of leafhopper vector benefits viral transmission . | NEW PHYTOLOGIST , 2024 , 243 (6) , 2368-2384 . |
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Arboviruses can be paternally transmitted by male insects to offspring for long-term persistence, but the mechanism remains largely unknown. Here, we use a model system of a destructive rice reovirus and its leafhopper vector to find that insect ribosome-rescuer Pelo-Hbs1 complex expressed on the sperm surface mediates paternal arbovirus transmission. This occurs through targeting virus-containing tubules constituted by viral nonstructural protein Pns11 to sperm surface via Pns11-Pelo interaction. Tubule assembly is dependent on Hsp70 activity, while Pelo-Hbs1 complex inhibits tubule assembly via suppressing Hsp70 activity. However, virus-activated ubiquitin ligase E3 mediates Pelo ubiquitinated degradation, synergistically causing Hbs1 degradation. Importantly, Pns11 effectively competes with Pelo for binding to E3, thus antagonizing E3-mediated Pelo-Hbs1 degradation. These processes cause a slight reduction of Pelo-Hbs1 complex in infected testes, promoting effective tubule assembly. Our findings provide insight into how insect sperm-specific Pelo-Hbs1 complex is modulated to promote paternal virus transmission without disrupting sperm function. In this study, Sun et al identify the leafhopper Pelo-Hbs1 complex in protein translational quality control as a sperm factor that mediates paternal arbovirus transmission to offspring without impairing sperm function, which contributes to long-term virus persistence in its natural vector.
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| GB/T 7714 | Sun, Xinyan , Du, Yu , Cheng, Yu et al. Insect ribosome-rescuer Pelo-Hbs1 complex on sperm surface mediates paternal arbovirus transmission [J]. | NATURE COMMUNICATIONS , 2024 , 15 (1) . |
| MLA | Sun, Xinyan et al. "Insect ribosome-rescuer Pelo-Hbs1 complex on sperm surface mediates paternal arbovirus transmission" . | NATURE COMMUNICATIONS 15 . 1 (2024) . |
| APA | Sun, Xinyan , Du, Yu , Cheng, Yu , Guan, Wang , Li, You , Chen, Hongyan et al. Insect ribosome-rescuer Pelo-Hbs1 complex on sperm surface mediates paternal arbovirus transmission . | NATURE COMMUNICATIONS , 2024 , 15 (1) . |
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