The nucleocapsid protein of rice stripe virus in cell nuclei of vector insect regulates viral replication

Zhao, Wan; Zhu, Jiachen; Liang, Hong; Zhu, Jiaming; Jiang, Fei; Wang, Wei; Li, Luo; Kang, Le; Cui, Feng

doi:10.1007/s13238-021-00822-1

Cited by 14 publications

(32 citation statements)

References 62 publications

(43 reference statements)

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“…S1A). As expected from previous work (26), the RSV amount in terms of the NP RNA level and viral genomic levels significantly increased in the whole bodies of viruliferous planthoppers at 8 d after ds3IMP-RNA delivery,…”

Section: Effect Of the Importin α Family On Rsv Transmission By Planthopperssupporting

confidence: 88%

“…Affinity through the Importin β-Binding Domain. In our previous work, importin α2 was found to interact in vitro with RSV NP (26,27). Here, we confirmed the contact of the two proteins in vivo through coimmunoprecipitation (Co-IP) assays using the monoclonal anti-NP antibody to pull down the complex of importin α2 and NP from the total protein of viruliferous planthoppers (Fig.…”

Section: Importin α2 Binds Viral Nucleocapsid Protein With a Relatively Highsupporting

confidence: 83%

“…Importin α1 and α3 did not affect RSV entry into salivary-gland cells. Our previous work showed that importin α3 was mainly localized in the nucleus and that the interaction of the three importin α proteins significantly affected RSV nuclear entry and replication, while single importin α did not have obvious effects in planthoppers (26). We speculate that importin α1 and α3 are the main players in regulating viral nuclear entry and that importin α2 is responsible for viral cell entry.…”

Section: Discussionmentioning

confidence: 78%

“…Importin α2 Is Localized in the Plasma Membrane. To explain the specific role of importin α2, we explored the localization of importin α2 in salivary-gland cells and midgut cells of viruliferous planthoppers with immunohistochemistry assays using polyclonal antibodies against importin α2 from our previous study (26). The orange was observed in the plasma membrane when the green importin α2 was merged with red F-actin, indicating that importin α2 was localized in the plasma membrane in addition to the cytoplasm in both tissues (Fig.…”

Section: Importin α2 Binds Viral Nucleocapsid Protein With a Relatively Highmentioning

confidence: 98%

“…In our recent work, we found that three importin α proteins, importin α1 (GenBank registration number MT036051), α2 (MT036050), and α3 (MT036052), of the small brown planthopper participate in the nuclear entry of RSV through direct interactions with RSV NPs, triggering an antiviral caspase-dependent apoptotic reaction (26). Knockdown of the expression of all the three importin α genes retarded the nuclear entry of RSV and led to an increase in viral load in planthoppers (26). However, we did not determine the influence on viral transmission.…”

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confidence: 99%

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Membrane association of importin α facilitates viral entry into salivary gland cells of vector insects

Liang

Wang

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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The importin α family belongs to the conserved nuclear transport pathway in eukaryotes. However, the biological functions of importin α in the plasma membrane are still elusive. Here, we report that importin α, as a plasma membrane–associated protein, is exploited by the rice stripe virus (RSV) to enter vector insect cells, especially salivary gland cells. When the expression of three importin α genes was simultaneously knocked down, few virions entered the salivary glands of the small brown planthopper, Laodelphax striatellus. Through hemocoel inoculation of virions, only importin α2 was found to efficiently regulate viral entry into insect salivary-gland cells. Importin α2 bound the nucleocapsid protein of RSV with a relatively high affinity through its importin β–binding (IBB) domain, with a dissociation constant KD of 9.1 μM. Furthermore, importin α2 and its IBB domain showed a distinct distribution in the plasma membrane through binding to heparin in heparan sulfate proteoglycan. When the expression of importin α2 was knocked down in viruliferous planthoppers or in nonviruliferous planthoppers before they acquired virions, the viral transmission efficiency of the vector insects in terms of the viral amount and disease incidence in rice was dramatically decreased. These findings not only reveal the specific function of the importin α family in the plasma membrane utilized by viruses, but also provide a promising target gene in vector insects for manipulation to efficiently control outbreaks of rice stripe disease.

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Section: Effect Of the Importin α Family On Rsv Transmission By Planthopperssupporting

confidence: 88%

Section: Importin α2 Binds Viral Nucleocapsid Protein With a Relatively Highsupporting

confidence: 83%

Section: Discussionmentioning

confidence: 78%

Section: Importin α2 Binds Viral Nucleocapsid Protein With a Relatively Highmentioning

confidence: 98%

mentioning

confidence: 99%

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Membrane association of importin α facilitates viral entry into salivary gland cells of vector insects

Liang

Wang

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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Discovery of Pyrido[1,2-a]pyrimidinone Mesoionic Compounds Incorporating a Dithioacetal Moiety as Novel Potential Insecticidal Agents

Zhang

Song

et al. 2021

J. Agric. Food Chem.

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A series of novel mesoionic pyrido[1,2-a]pyrimidinone compounds incorporating a dithioacetal skeleton were designed and synthesized for use as insecticidal agents. The biological activity of the title compounds indicated good to excellent insecticidal activities against bean aphids (Aphis craccivora) and white-backed planthoppers (Sogatella furcifera). Compound 34 showed excellent insecticidal activity against bean aphids (A. craccivora) with an LC50 value of 2.80 μg/mL, exceeding the insecticidal activity of trifluoropyrimidine (LC50 = 4.20 μg/mL). Proteomics and molecular docking results indicated that compound 34 could act on nicotinic acetylcholine receptors. This study provides support for the application of mesoionic pyrido[1,2-a]pyrimidinone compounds containing dithioacetal as novel insecticidal agents.

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Maintenance of persistent transmission of a plant arbovirus in its insect vector mediated by the Toll-Dorsal immune pathway

He,

Lu,

et al. 2024

Proc. Natl. Acad. Sci. U.S.A.

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Throughout evolution, arboviruses have developed various strategies to counteract the host’s innate immune defenses to maintain persistent transmission. Recent studies have shown that, in addition to bacteria and fungi, the innate Toll-Dorsal immune system also plays an essential role in preventing viral infections in invertebrates. However, whether the classical Toll immune pathway is involved in maintaining the homeostatic process to ensure the persistent and propagative transmission of arboviruses in insect vectors remain unclear. In this study, we revealed that the transcription factor Dorsal is actively involved in the antiviral defense of an insect vector ( Laodelphax striatellus ) by regulating the target gene, zinc finger protein 708 ( LsZN708 ), which mediates downstream immune-related effectors against infection with the plant virus (Rice stripe virus, RSV). In contrast, an antidefense strategy involving the use of the nonstructural-protein (NS4) to antagonize host antiviral defense through competitive binding to Dorsal from the MSK2 kinase was employed by RSV; this competitive binding inhibited Dorsal phosphorylation and reduced the antiviral response of the host insect. Our study revealed the molecular mechanism through which Toll-Dorsal-ZN708 mediates the maintenance of an arbovirus homeostasis in insect vectors. Specifically, ZN708 is a newly documented zinc finger protein targeted by Dorsal that mediates the downstream antiviral response. This study will contribute to our understanding of the successful transmission and spread of arboviruses in plant or invertebrate hosts.

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The nucleocapsid protein of rice stripe virus in cell nuclei of vector insect regulates viral replication

Cited by 14 publications

References 62 publications

Membrane association of importin α facilitates viral entry into salivary gland cells of vector insects

Membrane association of importin α facilitates viral entry into salivary gland cells of vector insects

Discovery of Pyrido[1,2-a]pyrimidinone Mesoionic Compounds Incorporating a Dithioacetal Moiety as Novel Potential Insecticidal Agents

Maintenance of persistent transmission of a plant arbovirus in its insect vector mediated by the Toll-Dorsal immune pathway

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