A glutathione-S-transferase (TuGSTd05) associated with acaricide resistance in Tetranychus urticae directly metabolizes the complex II inhibitor cyflumetofen

详细信息    查看全文

• 作者：Nena Pavlidi^a ; ^b ; Mousaalreza Khalighi^c ; Antonis Myridakis^d ; Wannes Dermauw^c ; Nicky Wybouw^b ; Dimitra Tsakireli^a ; ^e ; Euripides G. Stephanou^d ; Nikolaos E. Labrou^f ; John Vontas^e ; ^g ; ^{vontas@imbb.forth.gr} ; ^{vontas@aua.gr} ; Thomas Van Leeuwen^b ; ^c ; ^{thomas.vanleeuwen@ugent.be}
• 关键词：Cyflumetofen resistance ; Gene-expression microarray ; Glutathione S-transferase ; Metabolic detoxification ; Molecular docking ; Site-directed mutagenesis
• 刊名：Insect Biochemistry and Molecular Biology
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：80
• 期：Complete
• 页码：101-115
• 全文大小：2232 K
• 卷排序：80

文摘

TuGSTd05 is over-expressed in a cyflumetofen-resistant Tetranychus urticae strain. Cyflumetofen de-esterified metabolite is a strong inhibitor of GST activity in vitro. Recombinant enzyme catalyzes the conjugation of GSH to cyflumetofen/de-esterified metabolite. Site of attack, metabolite structure and key amino acids involved in the interaction were identified.