Functional Analysis of an Epsilon-Class Glutathione S-Transferase From Nilaparvata lugens (Hemiptera: Delphacidae). Issue 5 (13th October 2019)

• Record Type: Journal Article
• Authors: Saruta, Fumiko; Yamada, Naotaka; Yamamoto, Kohji
• Editors: Chiu, Joanna
• Is Part Of: Journal of insect science. Volume 19:Issue 5(2019)
• Publication Date: 2019-10-13
• Subjects: Nilaparvata lugens -- glutathione -- glutathione transferase -- insecticide -- site-directed mutagenesis; Insects -- Periodicals; Entomology -- Periodicals; Arthropoda -- Periodicals; Insects; Arthropods; Biology; Ecology; Entomologie -- Périodiques; Entomology; Insects; Electronic journals; Periodicals; 595.05
• DOI: 10.1093/jisesa/iez096
• Languages: English
• ISSNs: 1536-2442

Abstract

Abstract: Glutathione conjugation is a crucial step in xenobiotic detoxification. In the current study, we have functionally characterized an epsilon-class glutathione S-transferase (GST) from a brown planthopper Nilaparvata lugens (nlGSTE). The amino acid sequence of nlGSTE revealed approximately 36–44% identity with epsilon-class GSTs of other species. The recombinant nlGSTE was prepared in soluble form by bacterial expression and was purified to homogeneity. Mutation experiments revealed that the putative substrate-binding sites, including Phe107, Arg112, Phe118, and Phe119, were important for glutathione transferase activity. Furthermore, inhibition study displayed that nlGSTE activity was affected by insecticides, proposing that, in brown planthopper, nlGSTE could recognize insecticides as substrates.