Identification and functional analysis of a novel chorion protein essential for egg maturation in the brown planthopper

Lou, Yi-Han; Pan, Peng-Lu; Ye, Y.-X.; Cheng, Chen; Xu, Haijun; Zhang, Chuan‐Xi

doi:10.1111/imb.12380

Cited by 25 publications

(21 citation statements)

References 43 publications

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“…RNAi is an effective and widely used tool to regulate gene expression in the field of gene function research (Lou et al 2018). To verify the specificity and validity of dsG6Pase and dsHK activities in the brown planthopper, we examined the relative expression of G6Pase and HK after injection of dsG6Pase or dsHK.…”

Section: Discussionmentioning

confidence: 99%

Glucose Utilization in the Regulation of Chitin Synthesis in Brown Planthopper

Pan

et al. 2019

Journal of Insect Science

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Glucose-6-phosphatase (G6Pase) and hexokinase (HK) are two key enzymes in the glycolysis and gluconeogenesis pathways, which catalyze the synthesis and degradation of glucose in insects, respectively. G6Pase and HK play an important role in insect growth by regulating the metabolism of glucose, leading to the efficient metabolism of other macromolecules. However, it is unclear whether these genes could be investigated for pest control through their actions on chitin metabolism. We studied the potential functions of G6Pase and HK genes in the regulation of chitin metabolism pathways by RNAi technology. Interference with G6Pase expression did not affect trehalose and chitin metabolism pathways in brown planthopper, Nilaparvata lugens (Stål). However, knockdown of the HK gene resulted in a significant decrease of expression of genes associated with the trehalose metabolic pathway but had no significant effect on trehalase activity, trehalose content, or glucogen content. Additionally, HK knockdown resulting in downregulation of the genes involved in chitin metabolism in the brown planthopper. These insects also showed wing deformities and difficulty in molting to varying degrees. We suggest that the silencing of HK expression directly inhibited the decomposition of glucose, leading to impaired chitin synthesis.

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Section: Discussionmentioning

confidence: 99%

Glucose Utilization in the Regulation of Chitin Synthesis in Brown Planthopper

Pan

et al. 2019

Journal of Insect Science

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“…NlESMuc has a similar expression pattern to the known eggshell protein NlChP (Lou et al, 2018), however, we found some differences. NlChP expression started about 48 h after emergence in female adult BPH, while NlESMuc expression started about 24 h after emergence, indicating earlier transcription of NlESMuc .…”

Section: Discussionmentioning

confidence: 53%

A Mucin-Like Protein Is Essential for Oviposition in Nilaparvata lugens

Lou

Shen

et al. 2019

Front. Physiol.

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Mucins play a variety of roles; for example, in vertebrates, mucins lubricate epithelial surfaces and protect tissue from physical and biological damage, however, knowledge of insect mucins is limited. Here, we identified an eggshell-related mucin-like protein, NlESMuc, in the brown planthopper (BPH), Nilaparvata lugens . NlESMuc was specifically expressed in the follicular cells from the egg chambers of the ovarioles. RNA interference (RNAi) was used to perform functional analysis of NlESMuc . Adult female BPH with NlESMuc knockdown had significantly reduced fecundity, including more difficult oviposition, lower egg production, and eggs that could not hatch. Scanning electron microscopy showed that, in NlESMuc knocked-down BPH, the ultrastructure of the eggshells of fully developed oocytes was loose, and the cross-section showed many small droplets of about 0.1-μm diameter. Based on the results, it is concluded that NlESMuc is an eggshell-related protein and essential for normal oviposition. Our findings help to provide new targets for pesticide design and RNAi-based BPH control and will also provide new insights into insect eggshells and insect mucins.

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“…RNAi technology has become an effective tool in the research of insect gene function, gene expression regulation, pest control, and new pesticide development (Lou et al 2018;Han et al 2018). Although the brown planthopper is an agricultural pest, it is also a desirable model insect to study gene function (Xi et al 2015a, b).…”

Section: Discussionmentioning

confidence: 99%

Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens

Pan

Liu

et al. 2020

3 Biotech

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Phosphoglucomutase (PGM) is a key enzyme in glycolysis and gluconeogenesis, regulating both glycogen and trehalose metabolism in insects. In this study, we explored the potential function of phosphoglucomutase (PGM) using RNA interference technology in Nilaparvata lugens, the brown planthopper. PGM1 and PGM2 were found highly expressed in the midgut of brown planthoppers, with different expression levels in different instar nymphs. The glycogen, glucose, and trehalose levels were also significantly increased after brown planthoppers were injected with dsRNA targeting PGM1 (dsPGM1) or PGM2 (dsPGM2). In addition, injection of dsPGM1 or dsPGM2 resulted in increased membrane-bound trehalase activity but not soluble trehalase activity. Furthermore, the expression of genes related to trehalose and glycogen metabolism decreased significantly after injection with dsPGM1 and dsPGM2. The expression levels of genes involved in chitin metabolism in the brown planthopper were also significantly decreased and the insects showed wing deformities and difficulty molting following RNAi. We suggest that silencing of PGM1 and PGM2 expression directly inhibits trehalose metabolism, leading to impaired chitin synthesis.

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Identification and functional analysis of a novel chorion protein essential for egg maturation in the brown planthopper

Cited by 25 publications

References 43 publications

Glucose Utilization in the Regulation of Chitin Synthesis in Brown Planthopper

Glucose Utilization in the Regulation of Chitin Synthesis in Brown Planthopper

A Mucin-Like Protein Is Essential for Oviposition in Nilaparvata lugens

Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens

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