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Ä Ö Ü ä ö ü ß
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        Molecular identification and the role of adipokinetic hormone receptor in Helicoverpa armigera (Hübner)

        Xiao Zhengkun,Jin Ruoheng,Yun Tan,Tang Jun,Huang Guo-Hua 한국응용곤충학회 2023 Journal of Asia-Pacific Entomology Vol.26 No.2

        In insects, lipids and trehalose are the primary energy reserves and sources, and their metabolism is controlled by a variety of physiological processes. Adipokinetic hormone receptor (AKHR) has been reported to be involved in glycolipid metabolism and immune response, however, is an uncharted territory in Helicoverpa armigera. In the present study, the full-length cDNA encoding AKHR was isolated from H. armigera. The HaAKHR contains a seven-transmembrane domain, which was a characteristic of G-protein coupled receptors. The expression profile analysis revealed that HaAKHR was highly expressed in fat body of newly emerged female adults and highly expressed in the immature stage. The content of triglyceride (TAG) in fat body increased significantly after silencing of HaAKHR, however, the trehalase activity and the expression of trehalose-6-phosphate synthase (TPS) were decreased in hemolymph. Furthermore, the expression level of HaAKHR was significantly upregulated when infected with different kinds of entomopathogenic microbes. The above results suggested that HaAKHR plays an important role in regulating glycolipid metabolism and immune response in H. armigera, and contribute to understanding the underlying mechanism of host-pathogen interactions in H. armigera.

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        Expression, purification and enzymatic properties of a β-Nacetylhexosaminidase from brown planthopper, Nilaparvata lugens

        Yunhua Zhang,Jinyun Ji,Xiao Zhao,Ruoheng Jin,Jian Hong Li,Hu Wan 한국응용곤충학회 2017 Journal of Asia-Pacific Entomology Vol.20 No.4

        A previous study demonstrated that a β-N-acetyl-D-hexosaminidase (NlHex4) from the brown planthopper could serve as a new potential target for biopesticides due to its requirement for molting, and lethal phenotypes were observed via RNA interference. However, the enzymatic properties of NlHex4 remain unclear. In the present study, NlHex4 was expressed, purified and characterized. Recombinant NlHex4 was functionally expressed in baculovirus-infected insect cells and purified with a molecular weight of approximately 70 kDa. Recombinant NlHex4 had an optimal pH and temperature of 6.0 and 60 °C, respectively. Moreover, recombinant NlHex4 exhibited thermal stability at 50 °C for at least 1 h. Furthermore, the activity of recombinant NlHex4 was inhibited by the metal ions Fe2+ and Fe3+ and the serine protease inhibitor phenylmethanesulfonyl fluoride. These results reveal the enzymatic properties of NlHex4 and provide a basis for future investigation of the interaction between HEX and chitin oligosaccharide.

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