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学者姓名：张晓峰
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Abstract ：
Insect melanization triggered by the conversion of prophenoloxidase to active phenoloxidase via serine proteases (SPs) is an important immediate immune response. However, how phytoplasmas evade this immune response to promote their propagation in insect vectors remains unknown. Here, we demonstrate that infection of leafhopper vectors with rice orange leaf phytoplasma (ROLP) activates the mild melanization response in hemolymph. ROLP-encoded effector protein SRP1 is highly expressed in leafhopper hemolymph, where it competitively binds to SP2, thereby inhibiting SP2-mediated cleavage of prophenoloxidase into active phenoloxidase. Consequently, microinjection of SRP1 effectively suppresses the melanization response and enhances ROLP propagation. The histidine residue at position 23 of SRP1 is essential for SRP1-SP2 interaction, and the mutation of this position abolishes its ability to inhibit such SP2-meidated cleavage, ultimately promoting melanization response and inhibiting ROLP propagation. Our findings provide insights into how phytoplasmas antagonize insect melanization response to facilitate their persistent transmission.
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| GB/T 7714 | Zhang, Xiao-Feng , Li, Zhanpeng , Qiu, Jiaxin et al. A phytoplasma effector suppresses insect melanization immune response to promote pathogen persistent transmission [J]. | SCIENCE ADVANCES , 2025 , 11 (5) . |
| MLA | Zhang, Xiao-Feng et al. "A phytoplasma effector suppresses insect melanization immune response to promote pathogen persistent transmission" . | SCIENCE ADVANCES 11 . 5 (2025) . |
| APA | Zhang, Xiao-Feng , Li, Zhanpeng , Qiu, Jiaxin , Zhang, Ruonan , Jiang, Zhoumian , Wang, Tengfei et al. A phytoplasma effector suppresses insect melanization immune response to promote pathogen persistent transmission . | SCIENCE ADVANCES , 2025 , 11 (5) . |
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The citrus disease Huanglongbing (HLB) in Asia and the US is caused by Candidatus Liberibacter asiaticus (CLas), which is primarily transmitted by Diaphorina citri, also known as Asian citrus psyllid in a persistent and propagative manner. However, the exact mechanisms underlying CLas circulation within D. citri remain largely unclear. Here, immunofluorescence microscopy and electron microscopy were utilized to track the sequential infection of CLas in D. citri, from alimentary canal to salivary glands, and ultimately to the plant host. CLas was found to initially infect the epithelium of filter chamber, after which it rapidly spreads to visceral muscles for further infection throughout the alimentary canal. The rapid spread in D. citri adults causes the duration of CLas circulation to be as short as 9 days. The duration of latent period may be explained by the recruitment of cytoskeletal alpha-actinin by the outer membrane protein (OMP) of CLas. Inhibition of actin filament or knocking down the expression of alpha-actinin significantly suppresses CLas cytoskeleton-dependent infection in and spread among D. citri organs. Injection of prokaryotically expressed OMP into D. citri also recruits alpha-actinin, resembling the natural infection of CLas. Our studies showed that CLas exploits alpha-actinin and remolds actin machinery of D. citri for overcoming the midgut release barrier, facilitating its circulation in the vector. By shedding light on these mechanisms, this report reveals more detailed mechanisms in CLas infection in D. citri, and offers a plausible explanation for rapid dissemination of HLB in nature from the perspective of psyllid transmission.
Keyword ：
Candidatus Liberibacter asiaticus Candidatus Liberibacter asiaticus Circulative infection Circulative infection Cytoskeleton Cytoskeleton Diaphorina citri Diaphorina citri
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| GB/T 7714 | Li, Zhiqiang , Yang, Xiao , Guo, Yuxin et al. Candidatus Liberibacter asiaticus exploits cytoskeletal system of psyllid vector for circulative propagative infection [J]. | MICROBIOLOGICAL RESEARCH , 2025 , 292 . |
| MLA | Li, Zhiqiang et al. "Candidatus Liberibacter asiaticus exploits cytoskeletal system of psyllid vector for circulative propagative infection" . | MICROBIOLOGICAL RESEARCH 292 (2025) . |
| APA | Li, Zhiqiang , Yang, Xiao , Guo, Yuxin , Zhang, Xiaofeng , Li, You , Kuo, Yen-Wen et al. Candidatus Liberibacter asiaticus exploits cytoskeletal system of psyllid vector for circulative propagative infection . | MICROBIOLOGICAL RESEARCH , 2025 , 292 . |
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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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Leaf yellowing is a well- known phenotype that attracts phloem- feeding insects. However, facilitate their own transmission by insect vectors. Here, we report that an effector protein secreted by rice orange leaf phytoplasma (ROLP) inhibits chlorophyll biosynthesis and induces leaf yellowing to attract leafhopper vectors, thereby presumably promoting pathogen transmission. This effector, designated secreted ROLP protein 1 (SRP1), first secreted into rice phloem by ROLP, was subsequently translocated to chloroplasts by interacting with the chloroplastic glutamine synthetase (GS2). The direct interaction between SRP1 and GS2 disrupts the decamer formation of the GS2 holoenzyme, attenuating its enzymatic activity, thereby suppressing the synthesis of chlorophyll precursors glutamate and glutamine. Transgenic expression of SRP1 in rice plants decreased GS2 activity and chlorophyll precursor accumulation, finally inducing leaf yellowing. This process is correlated with the previous evidence that the knockout of GS2 expression in rice plants causes a similar yellow chlorosis phenotype. Consistently, these yellowing leaves attracted higher numbers of leafhopper vectors, caused the vectors to probe more frequently, and presumably facilitate more efficient phytoplasma transmission. Together, these results uncover the mechanism used by phytoplasmas to manipulate the leaf color of infected plants for the purpose of enhancing attractiveness to insect vectors.
Keyword ：
effector protein effector protein insect attractiveness insect attractiveness leaf yellowing leaf yellowing OsGS2 OsGS2 ROLP ROLP
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| GB/T 7714 | Zhang, Xiao-Feng , Li, Zhanpeng , Lin, Hanbin et al. A phytoplasma effector destabilizes chloroplastic glutamine synthetase inducing chlorotic leaves that attract leafhopper vectors [J]. | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA , 2024 , 121 (22) . |
| MLA | Zhang, Xiao-Feng et al. "A phytoplasma effector destabilizes chloroplastic glutamine synthetase inducing chlorotic leaves that attract leafhopper vectors" . | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 121 . 22 (2024) . |
| APA | Zhang, Xiao-Feng , Li, Zhanpeng , Lin, Hanbin , Cheng, Yu , Wang, Huanqin , Jiang, Zhoumian et al. A phytoplasma effector destabilizes chloroplastic glutamine synthetase inducing chlorotic leaves that attract leafhopper vectors . | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA , 2024 , 121 (22) . |
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Plant jasmonoyl-L-isoleucine (JA-Ile) is a major defense signal against insect feeding, but whether or how insect salivary effectors suppress JA-Ile synthesis and thus facilitate viral transmission in the plant phloem remains elusive. Insect carboxylesterases (CarEs) are the third major family of detoxification enzymes. Here, we identify a new leafhopper CarE, CarE10, that is specifically expressed in salivary glands and is secreted into the rice phloem as a saliva component. Leafhopper CarE10 directly binds to rice jasmonate resistant 1 (JAR1) and promotes its degradation by the proteasome system. Moreover, the direct association of CarE10 with JAR1 clearly impairs JAR1 enzyme activity for conversion of JA to JA-Ile in an in vitro JAIle synthesis system. A devastating rice reovirus activates and promotes the co-secretion of virions and CarE10 via virus-induced vesicles into the saliva-storing salivary cavities of the leafhopper vector and ultimately into the rice phloem to establish initial infection. Furthermore, a virus-mediated increase in CarE10 secretion or overexpression of CarE10 in transgenic rice plants causes reduced levels of JAR1 and thus suppresses JA-Ile synthesis, promoting host attractiveness to insect vectors and facilitating initial viral transmission. Our findings provide insight into how the insect salivary protein CarE10 suppresses host JA-Ile synthesis to promote initial virus transmission in the rice phloem.
Keyword ：
initial viral transmission initial viral transmission JA-Ile synthesis JA-Ile synthesis JAR1 degradation JAR1 degradation leafhopper leafhopper rice phloem rice phloem salivary protein CarE10 salivary protein CarE10
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| GB/T 7714 | Chi, Yunhua , Zhang, Hongxiang , Chen, Siyu et al. Leafhopper salivary carboxylesterase suppresses JA-Ile synthesis to facilitate initial arbovirus transmission in rice phloem [J]. | PLANT COMMUNICATIONS , 2024 , 5 (9) . |
| MLA | Chi, Yunhua et al. "Leafhopper salivary carboxylesterase suppresses JA-Ile synthesis to facilitate initial arbovirus transmission in rice phloem" . | PLANT COMMUNICATIONS 5 . 9 (2024) . |
| APA | Chi, Yunhua , Zhang, Hongxiang , Chen, Siyu , Cheng, Yu , Zhang, Xiaofeng , Jia, Dongsheng et al. Leafhopper salivary carboxylesterase suppresses JA-Ile synthesis to facilitate initial arbovirus transmission in rice phloem . | PLANT COMMUNICATIONS , 2024 , 5 (9) . |
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Rice yellow stunt virus (RYSV) P3 protein functions as a movement protein during viral infection of a plant host; its function in insect hosts remains unclear. In this study, we investigated the subcellular localization of P3 using leafhopper (Nephotettix cincticeps) cell cultures. Our results showed that P3 translocated from the cytoplasm to the nucleus in RYSV-infected leafhopper cells, where it interacted with the viral N protein as a constituent of viroplasms. Interfering with the P3 gene expression significantly suppressed viral infection in N. cincticeps. Finally, we demonstrate that the nuclear translocation of P3 in leafhopper cells depended on its interaction with RYSV N protein, which enters the nucleus via an interaction with importin alpha 3. These findings unveil a previously unknown role for P3 in RYSV infection of the insect vector and provide valuable insights into the infection dynamics of plant rhabdoviruses.
Keyword ：
Importin alpha 3 Importin alpha 3 Insect vector Insect vector P3 protein P3 protein Rice yellow stunt virus Rice yellow stunt virus Viroplasm Viroplasm
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| GB/T 7714 | Huang, Zhejun , Ji, Zhenxi , Wang, Juan et al. Rice yellow stunt virus p3 protein enters the nucleus of leafhopper cell and localizes to viroplasm through interaction with N protein via importin α3-mediated pathway [J]. | PHYTOPATHOLOGY RESEARCH , 2023 , 5 (1) . |
| MLA | Huang, Zhejun et al. "Rice yellow stunt virus p3 protein enters the nucleus of leafhopper cell and localizes to viroplasm through interaction with N protein via importin α3-mediated pathway" . | PHYTOPATHOLOGY RESEARCH 5 . 1 (2023) . |
| APA | Huang, Zhejun , Ji, Zhenxi , Wang, Juan , Li, Zhanpeng , Jiang, Zhoumian , Ni, Wei et al. Rice yellow stunt virus p3 protein enters the nucleus of leafhopper cell and localizes to viroplasm through interaction with N protein via importin α3-mediated pathway . | PHYTOPATHOLOGY RESEARCH , 2023 , 5 (1) . |
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Multiple viral infections in insect vectors with synergistic effects are common in nature, but the underlying mechanism remains elusive. Here, we find that rice gall dwarf reovirus (RGDV) facilitates the transmission of rice stripe mosaic rhabdovirus (RSMV) by co-infected leafhopper vectors. RSMV nucleoprotein (N) alone activates complete anti-viral autophagy, while RGDV nonstructural protein Pns11 alone induces pro-viral incomplete autophagy. In co-infected vectors, RSMV exploits Pns11-induced autophagosomes to assemble enveloped virions via N-Pns11-ATG5 interaction. Furthermore, RSMV could effectively propagate in Sf9 cells. Expression of Pns11 in Sf9 cells or leafhopper vectors causes the recruitment of N from the ER to Pns11-induced autophagosomes and inhibits N-induced complete autophagic flux, finally facilitating RSMV propagation. In summary, these results demonstrate a previously unappreciated role of autophagy in the regulation of the direct synergistic interaction during co-transmission of two distinct arboviruses by insect vectors and reveal the functional importance of virus-induced autophagosomes in rhabdovirus assembly.
Keyword ：
autophagy autophagy co-transmission co-transmission insect vector insect vector rhabdovirus rhabdovirus synergistic interaction synergistic interaction
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| GB/T 7714 | Jia, Dongsheng , Liang, Qifu , Chen, Hongyan et al. Autophagy mediates a direct synergistic interaction during co-transmission of two distinct arboviruses by insect vectors [J]. | SCIENCE CHINA-LIFE SCIENCES , 2023 , 66 (7) : 1665-1681 . |
| MLA | Jia, Dongsheng et al. "Autophagy mediates a direct synergistic interaction during co-transmission of two distinct arboviruses by insect vectors" . | SCIENCE CHINA-LIFE SCIENCES 66 . 7 (2023) : 1665-1681 . |
| APA | Jia, Dongsheng , Liang, Qifu , Chen, Hongyan , Liu, Huan , Li, Guangjun , Zhang, Xiaofeng et al. Autophagy mediates a direct synergistic interaction during co-transmission of two distinct arboviruses by insect vectors . | SCIENCE CHINA-LIFE SCIENCES , 2023 , 66 (7) , 1665-1681 . |
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Both viruses and host cells compete for intracellular polyamines for efficient propagation. Currently, how the key polyamine-metabolizing enzymes, including ornithine decarboxylase 1 (ODC1) and its antizyme 1 (OAZ1), are activated to co-ordinate viral propagation and polyamine biosynthesis remains unknown. Here, we report that the matrix protein of rice stripe mosaic virus (RSMV), a cytorhabdovirus, directly hijacks OAZ1 to ensure the proper assembly of rigid bacilliform non-enveloped virions in leafhopper vector. Viral matrix protein effectively competes with ODC1 to bind to OAZ1, and thus, the ability of OAZ1 to target and mediate the degradation of ODC1 is significantly inhibited during viral propagation, which finally promotes polyamines production. Thus, OAZ1 and ODC1 are activated to synergistically promote viral persistent propagation and polyamine biosynthesis in viruliferous vectors. Our data suggest that it is a novel mechanism for rhabdovirus to exploit OAZ1 for facilitating viral assembly.
Keyword ：
Insect vector Insect vector OAZ1 OAZ1 ODC1 ODC1 Polyamines Polyamines Rhabdovirus Rhabdovirus Rice stripe mosaic virus Rice stripe mosaic virus Viral assembly Viral assembly
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| GB/T 7714 | Jia, Dongsheng , Liu, Huan , Zhang, Jian et al. Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors [J]. | STRESS BIOLOGY , 2022 , 2 (1) . |
| MLA | Jia, Dongsheng et al. "Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors" . | STRESS BIOLOGY 2 . 1 (2022) . |
| APA | Jia, Dongsheng , Liu, Huan , Zhang, Jian , Wan, Wenqiang , Wang, Zongwen , Zhang, Xiaofeng et al. Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors . | STRESS BIOLOGY , 2022 , 2 (1) . |
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Rice stripe mosaic virus (RSMV), a newly discovered plant cytorhabdovirus, and rice gall dwarf virus (RGDV), a plant reovirus, are transmitted by leafhopper Recilia dorsalis in a persistent-propagative manner. In this study, field surveys in Luoding city, Guangdong province of southern China, showed that RSMV and RGDV frequently co-infected rice plants. Furthermore, this co-infection had a synergistic effect on viral replication potential and pathogenicity in rice plants. Meanwhile, RSMV and RGDV also co-infected R. dorsalis vectors, and RGDV significantly promoted the propagation of RSMV in co-infected vectors. Accordingly, co-infection significantly promoted the acquisition and transmission efficiencies of RSMV by R. dorsalis. However, such co-infection did not significantly affect the propagation of RGDV in vectors. More importantly, we also observed that non-viruliferous R. dorsalis preferred to feed on co-infected rice plants, and this process further affected the feeding behavior of R. dorsalis to enhance viral release into rice phloem. These results provided the clues as to why RSMV had been a gradually expanding problem, creating an increasing risk of damage to rice production. Our findings revealed that synergism between RSMV and RGDV in their host and vector enhanced the propagation and transmission of RSMV, which will help guide the formulation of viral control strategies.
Keyword ：
co-infection co-infection Recilia dorsalis Recilia dorsalis rice gall dwarf virus rice gall dwarf virus rice stripe mosaic virus rice stripe mosaic virus synergism synergism transmission transmission
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| GB/T 7714 | Jia, Dongsheng , Luo, Guozhong , Shi, Wei et al. Rice Gall Dwarf Virus Promotes the Propagation and Transmission of Rice Stripe Mosaic Virus by Co-infected Insect Vectors [J]. | FRONTIERS IN MICROBIOLOGY , 2022 , 13 . |
| MLA | Jia, Dongsheng et al. "Rice Gall Dwarf Virus Promotes the Propagation and Transmission of Rice Stripe Mosaic Virus by Co-infected Insect Vectors" . | FRONTIERS IN MICROBIOLOGY 13 (2022) . |
| APA | Jia, Dongsheng , Luo, Guozhong , Shi, Wei , Liu, Ye , Liu, Huan , Zhang, Xiaofeng et al. Rice Gall Dwarf Virus Promotes the Propagation and Transmission of Rice Stripe Mosaic Virus by Co-infected Insect Vectors . | FRONTIERS IN MICROBIOLOGY , 2022 , 13 . |
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Author summaryNumerous plant viruses replicate inside the cells of their insect vectors. Here, we demonstrate that the progeny virions of rice gall dwarf virus in leafhopper vector are engulfed within virus-induced double-membraned autophagosomes. Such autophagosomes are modified to evade degradation, thus can be persistently exploited by viruses to safely transport virions across multiple insect membrane barriers. Viral nonstructural protein Pns11 induces the formation of autophagosomes via interaction with ATG5, and potentially blocks autophagosome degradation via mediating the reduced expression of N-glycosylated Lamp1 on lysosomal membranes. For the first time, we reveal that a nonstructural protein encoded by a persistent plant virus can induce an incomplete autophagy to benefit viral propagation in its insect vectors. Viruses can hijack autophagosomes as the nonlytic release vehicles in cultured host cells. However, how autophagosome-mediated viral spread occurs in infected host tissues or organs in vivo remains poorly understood. Here, we report that an important rice reovirus, rice gall dwarf virus (RGDV) hijacks autophagosomes to traverse multiple insect membrane barriers in the midgut and salivary gland of leafhopper vector to enhance viral spread. Such virus-containing double-membraned autophagosomes are prevented from degradation, resulting in increased viral propagation. Mechanistically, viral nonstructural protein Pns11 induces autophagy and embeds itself in the autophagosome membranes. The autophagy-related protein 5 (ATG5)-ATG12 conjugation is essential for initial autophagosome membrane biogenesis. RGDV Pns11 specifically interacts with ATG5, both in vitro and in vivo. Silencing of ATG5 or Pns11 expression suppresses ATG8 lipidation, autophagosome formation, and efficient viral propagation. Thus, Pns11 could directly recruit ATG5-ATG12 conjugation to induce the formation of autophagosomes, facilitating viral spread within the insect bodies. Furthermore, Pns11 potentially blocks autophagosome degradation by directly targeting and mediating the reduced expression of N-glycosylated Lamp1 on lysosomal membranes. Taken together, these results highlight how RGDV remodels autophagosomes to benefit viral propagation in its insect vector.
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| GB/T 7714 | Jia, Dongsheng , Liang, Qifu , Liu, Huan et al. A nonstructural protein encoded by a rice reovirus induces an incomplete autophagy to promote viral spread in insect vectors [J]. | PLOS PATHOGENS , 2022 , 18 (5) . |
| MLA | Jia, Dongsheng et al. "A nonstructural protein encoded by a rice reovirus induces an incomplete autophagy to promote viral spread in insect vectors" . | PLOS PATHOGENS 18 . 5 (2022) . |
| APA | Jia, Dongsheng , Liang, Qifu , Liu, Huan , Li, Guangjun , Zhang, Xiaofeng , Chen, Qian et al. A nonstructural protein encoded by a rice reovirus induces an incomplete autophagy to promote viral spread in insect vectors . | PLOS PATHOGENS , 2022 , 18 (5) . |
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