A glutathione S-transferase PcGSTMu2 involved in the detoxification of bifenazate in Panonychus citri.

Autor: Li MY; Citrus Research Institute, Southwest University, National Citrus Engineering Research Center, Chongqing, China., Cheng LY; Citrus Research Institute, Southwest University, National Citrus Engineering Research Center, Chongqing, China.; Shenzhen Institute of Standards and Technology, Shenzhen, China., Li SC; Citrus Research Institute, Southwest University, National Citrus Engineering Research Center, Chongqing, China., Fang YH; Citrus Research Institute, Southwest University, National Citrus Engineering Research Center, Chongqing, China., Shao BB; Citrus Research Institute, Southwest University, National Citrus Engineering Research Center, Chongqing, China., Cui YY; Citrus Research Institute, Southwest University, National Citrus Engineering Research Center, Chongqing, China., Wei ZT; Citrus Research Institute, Southwest University, National Citrus Engineering Research Center, Chongqing, China., Yu SJ; Citrus Research Institute, Southwest University, National Citrus Engineering Research Center, Chongqing, China., Ran C; Citrus Research Institute, Southwest University, National Citrus Engineering Research Center, Chongqing, China.
Jazyk: angličtina
Zdroj: Pest management science [Pest Manag Sci] 2025 Jan; Vol. 81 (1), pp. 372-383. Date of Electronic Publication: 2024 Sep 30.
DOI: 10.1002/ps.8440
Abstrakt: Background: The citri red mite, Panonychus citri (McGregor), is an important citrus pest worldwide, causing enormous economic losses to citrus production. Bifenazate is a widely used acaricide for controlling P. citri. The detoxification mechanism of bifenazate is not clear in P. citri.
Results: PcGSTMu2, a significantly upregulated GST gene, was identified by the transcriptome analysis of P. citri after bifenazate exposure. The expression level of PcGSTMu2 was significantly increased after bifenazate exposure. By using RNAi of PcGSTMu2, the susceptibility of P. citri to bifenazate was significantly increased. Protein modeling and docking of PcGSTMu2 with GSH and bifenazate indicated the potential amino acid residues for binding in the active site. Heterologous expression and in vitro functional assays further revealed that PcGSTMu2 could deplete bifenazate.
Conclusion: These results indicated that PcGSTMu2 plays an important role in the detoxification of bifenazate in P. citri and provides the molecular foundation for understanding bifenazate metabolism in P. citri. © 2024 Society of Chemical Industry.
(© 2024 Society of Chemical Industry.)
Databáze: MEDLINE
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