A glutathione S-transferase (BdGSTd9) participates in malathion resistance via directly depleting malathion and its toxic oxide malaoxon in Bactrocera dorsalis (Hendel).
Bactrocera dorsalis
HPLC
RNAi
glutathione S-transferases
insecticide resistance
malaoxon
malathion
Journal
Pest management science
ISSN: 1526-4998
Titre abrégé: Pest Manag Sci
Pays: England
ID NLM: 100898744
Informations de publication
Date de publication:
Aug 2020
Aug 2020
Historique:
received:
18
12
2019
revised:
23
02
2020
accepted:
03
03
2020
pubmed:
5
3
2020
medline:
9
9
2020
entrez:
5
3
2020
Statut:
ppublish
Résumé
The oriental fruit fly, Bactrocera dorsalis (Hendel), is a widespread agricultural pest that has evolved resistance to many commonly used insecticides including malathion. Glutathione S-transferases (GSTs) are multifunctional enzymes that metabolize insecticides directly or indirectly. The specific mechanism used by GSTs to confer malathion resistance in B. dorsalis is unclear. BdGSTd9 was identified from B. dorsalis and was expressed at twice the level in a malathion-resistant strain (MR) than in a susceptible strain (MS). By using RNAi of BdGSTd9, the toxicity of malathion against MR was increased. Protein modelling and docking of BdGSTd9 with malathion and malaoxon indicated key amino acid residues for direct binding in the active site. In vitro assays with engineered Sf9 cells overexpressing BdGSTd9 demonstrated lower cytotoxicity of malathion. High performance liquid chromatography (HPLC) analysis indicated that malathion could be broken down significantly by BdGSTd9, and it also could deplete the malathion metabolite malaoxon, which possesses a higher toxicity to B. dorsalis. Taken together, the BdGSTd9 of B. dorsalis could not only deplete malathion, but also react with malaoxon and therefore enhance malathion resistance. BdGSTd9 is a component of malathion resistance in B. dorsalis. It acts by depleting both malathion and malaoxon. © 2020 Society of Chemical Industry.
Sections du résumé
BACKGROUND
BACKGROUND
The oriental fruit fly, Bactrocera dorsalis (Hendel), is a widespread agricultural pest that has evolved resistance to many commonly used insecticides including malathion. Glutathione S-transferases (GSTs) are multifunctional enzymes that metabolize insecticides directly or indirectly. The specific mechanism used by GSTs to confer malathion resistance in B. dorsalis is unclear.
RESULTS
RESULTS
BdGSTd9 was identified from B. dorsalis and was expressed at twice the level in a malathion-resistant strain (MR) than in a susceptible strain (MS). By using RNAi of BdGSTd9, the toxicity of malathion against MR was increased. Protein modelling and docking of BdGSTd9 with malathion and malaoxon indicated key amino acid residues for direct binding in the active site. In vitro assays with engineered Sf9 cells overexpressing BdGSTd9 demonstrated lower cytotoxicity of malathion. High performance liquid chromatography (HPLC) analysis indicated that malathion could be broken down significantly by BdGSTd9, and it also could deplete the malathion metabolite malaoxon, which possesses a higher toxicity to B. dorsalis. Taken together, the BdGSTd9 of B. dorsalis could not only deplete malathion, but also react with malaoxon and therefore enhance malathion resistance.
CONCLUSION
CONCLUSIONS
BdGSTd9 is a component of malathion resistance in B. dorsalis. It acts by depleting both malathion and malaoxon. © 2020 Society of Chemical Industry.
Substances chimiques
Insecticides
0
Oxides
0
malaoxon
2439JYF84Q
Glutathione Transferase
EC 2.5.1.18
Malathion
U5N7SU872W
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
2557-2568Subventions
Organisme : Modern Agro-industry (Citrus) Technology Research System of China
Organisme : Foundation Project of Southwest University
Organisme : Chongqing Research Program of Basic Research and Frontier Technology
Organisme : National Student's Program for Innovation and Entrepreneurship Training Program
Organisme : National Key Research and Development Project
Informations de copyright
© 2020 Society of Chemical Industry.
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