scholarly journals Functional Analysis of an Epsilon-Class Glutathione S-Transferase From Nilaparvata lugens (Hemiptera: Delphacidae)

2019 ◽  
Vol 19 (5) ◽  
Author(s):  
Fumiko Saruta ◽  
Naotaka Yamada ◽  
Kohji Yamamoto
Keyword(s):  
Binding Sites ◽  
Glutathione Transferase ◽  
Brown Planthopper ◽  
Nilaparvata Lugens ◽  
Soluble Form ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Inhibition Study ◽  
Xenobiotic Detoxification ◽  
Substrate Binding Sites

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.

Purification, molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the rice brown planthopper, Nilaparvata lugens

2002 ◽  
Vol 362 (2) ◽  
pp. 329-337 ◽  
Author(s):  
John G. VONTAS ◽  
Graham J. SMALL ◽  
Dimitra C. NIKOU ◽  
Hilary RANSON ◽  
Janet HEMINGWAY
Keyword(s):  
Insecticide Resistance ◽  
Peroxidase Activity ◽  
Pyrethroid Resistance ◽  
Brown Planthopper ◽  
Resistance Mechanism ◽  
Amino Acid Identity ◽  
Nilaparvata Lugens ◽  
Northern Analysis ◽  
Affinity Column ◽  
Glutathione S Transferase

A novel glutathione S-transferase (GST)-based pyrethroid resistance mechanism was recently identified in Nilaparvata lugens [Vontas, Small and Hemingway (2001) Biochem. J. 357, 65–72]. To determine the nature of GSTs involved in conferring this resistance, the GSTs from resistant and susceptible strains of N. lugens were partially purified by anion exchange and affinity chromatography. The majority of peroxidase activity, previously correlated with resistance, was confined to the fraction that bound to the affinity column, which was considerably elevated in the resistant insects. A cDNA clone encoding a GST (nlgst1-1) —the first reported GST sequence from Hemiptera with up to 54% deduced amino-acid identity with other insect class I GSTs—was isolated from a pyrethroid-resistant strain. Northern analysis showed that nlgst1-1 was overexpressed in resistant insects. nlgst1-1 was expressed in Escherichia coli, purified and characterized. The ability of the recombinant protein to bind to the S-hexylglutathione affinity matrix, its substrate specificities and its immunological properties confirmed that this GST was one from the elevated subset of N. lugens GSTs. Peroxidase activity of the recombinant nlgst1-1 indicated that it had a role in resistance, through detoxification of lipid peroxidation products induced by pyrethroids. Southern analysis of genomic DNA from the resistant and susceptible strains indicated that GST-based insecticide resistance may be associated with gene amplification in N. lugens.

Interaction of Ferulic Acid with Glutathione S-Transferase and Carboxylesterase Genes in the Brown Planthopper, Nilaparvata lugens

2017 ◽  
Vol 43 (7) ◽  
pp. 693-702 ◽  
Author(s):  
Jun Yang ◽  
Xiao-Qin Sun ◽  
Shu-Ying Yan ◽  
Wen-Jun Pan ◽  
Mao-Xin Zhang ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Brown Planthopper ◽  
Nilaparvata Lugens ◽  
Glutathione S Transferase

scholarly journals The Key Glutathione S-Transferase Family Genes Involved in the Detoxification of Rice Gramine in Brown Planthopper Nilaparvata lugens

Insects ◽  
2021 ◽  
Vol 12 (12) ◽  
pp. 1055
Author(s):  
Jun Yang ◽  
Xiang-Dong Kong ◽  
Keyan Zhu-Salzman ◽  
Qing-Ming Qin ◽  
Qing-Nian Cai
Keyword(s):  
Brown Planthopper ◽  
Nilaparvata Lugens ◽  
Molecular Evidence ◽  
Glutathione S Transferase ◽  
Defensive Strategy ◽  
Detoxification Enzyme ◽  
Coevolution Theory ◽  
Glutathione S Transferases ◽  
Nilaparvata Lugens Stål ◽  
Insight Into

Phytochemical toxins are considered a defense measure for herbivore invasion. To adapt this defensive strategy, herbivores use glutathione S-transferases (GSTs) as an important detoxification enzyme to cope with toxic compounds, but the underlying molecular basis for GST genes in this process remains unclear. Here, we investigated the basis of how GST genes in brown planthopper (BPH, Nilaparvata lugens (Stål)) participated in the detoxification of gramine by RNA interference. For BPH, the LC25 and LC50 concentrations of gramine were 7.11 and 14.99 μg/mL at 72 h after feeding, respectively. The transcriptions of seven of eight GST genes in BPH were induced by a low concentration of gramine, and GST activity was activated. Although interferences of seven genes reduced BPH tolerance to gramine, only the expression of NlGST1-1, NlGSTD2, and NlGSTE1 was positively correlated with GST activities, and silencing of these three genes inhibited GST activities in BPH. Our findings reveal that two new key genes, NlGSTD2 and NlGSTE1, play an essential role in the detoxification of gramine such as NlGST1-1 does in BPH, which not only provides the molecular evidence for the coevolution theory, but also provides new insight into the development of an environmentally friendly strategy for herbivore population management.

Location of Substrate Binding Sites within the Integral Membrane Protein Microsomal Glutathione Transferase-1†

Biochemistry ◽  
2007 ◽  
Vol 46 (10) ◽  
pp. 2812-2822 ◽  
Author(s):  
Laura S. Busenlehner ◽  
Johan Ålander ◽  
Caroline Jegerscöhld ◽  
Peter J. Holm ◽  
Priyaranjan Bhakat ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Binding Sites ◽  
Glutathione Transferase ◽  
Substrate Binding ◽  
Integral Membrane Protein ◽  
Substrate Binding Sites ◽  
Microsomal Glutathione

Antifeedant and Insecticidal Effects of Mandelic Acid on the Brown Planthopper Nilaparvata lugens Stål

2011 ◽  
Vol 66 (9-10) ◽  
pp. 499-506
Author(s):  
Liang Jin ◽  
Pei-ying Hao ◽  
Sheng-zhang Dong ◽  
Ya-lin Bian ◽  
Ya-lin Bian ◽  
...  
Keyword(s):  
Survival Rate ◽  
Mandelic Acid ◽  
Brown Planthopper ◽  
Nilaparvata Lugens ◽  
Feeding Time ◽  
Transferase Activity ◽  
Electrical Penetration Graph ◽  
Insecticidal Effect ◽  
Glutathione Peroxidases ◽  
Nilaparvata Lugens Stål

To study the effects of mandelic acid (MA) on the brown planthopper (BPH), Nilaparvata lugens, the survival rate and behaviour of BPH fed on an artifi cial diet with different dosages of MA was observed. The survival rate of BPH decreased with the increase of the MA concentration and feeding time. In contrast to the control, the survival rate of BPH 72 h after feeding decreased signifi cantly. Electrical penetration graph (EPG) data indicated that MA absorbed by the rice plant from Kimura B solution signifi cantly affected the feeding behaviour of BPH. At the concentrations of 0.1, 0.5, and 1.0 mg/ml, duration of the phloem ingestion of BPH decreased from 115.34 min (control) to 30.41, 7.63, and 0.36 min, respectively. Periods of xylem ingestion of MA-treated BPH were signifi cantly shorter than those of the control (50.44 min). Moreover, BPH spent more time walking around or being at rest on MA-treated rice plants, as well as in stylet activities. The GST (glutathione S-transferase) activity of BPH increased with the increasing MA concentration, while the GPX (glutathione peroxidases) activity did not change signifi cantly. The results indicate that MA has an antifeedant and insecticidal effect on BPH.

Screening of rice genotypes for resistance to the brown planthopper, Nilaparvata lugens Stål

2012 ◽  
Vol 40 (4) ◽  
pp. 502-508 ◽  
Author(s):  
M. P. Ali ◽  
Salem S. Alghamdi ◽  
M. A. Begum ◽  
A. B. M. Anwar Uddin ◽  
M. Z. Alam ◽  
...  
Keyword(s):  
Brown Planthopper ◽  
Nilaparvata Lugens ◽  
Rice Genotypes
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