Evaluations of two glutathione S-transferase epsilon genes for their contributions to metabolism of three selected insecticides in Locusta migratoria

被引:11
作者
Zhang, Jianqin [1 ]
Ma, Wen [1 ]
Yin, Fei [1 ]
Park, Yoonseong [2 ]
Zhu, Kun Yan [2 ]
Zhang, Xueyao [3 ]
Qin, Xuemei [1 ]
Li, Daqi [4 ]
机构
[1] Shanxi Univ, Modern Res Ctr Tradit Chinese Med, Taiyuan 030006, Peoples R China
[2] Kansas State Univ, Dept Entomol, Manhattan, KS 66506 USA
[3] Shanxi Univ, Inst Appl Biol, Taiyuan 030006, Peoples R China
[4] Shanxi Agr Univ, Coll Plant Protect, Taiyuan 030031, Peoples R China
基金
中国国家自然科学基金;
关键词
Glutathione S-transferase; Insecticide detoxification; Locusta migratoria; Malathion; Recombinant enzyme; ANOPHELES-GAMBIAE; RESISTANCE; DETOXIFICATION; DDT; EXPRESSION; IDENTIFICATION; DROSOPHILA; VECTOR; STRAIN; GSTS;
D O I
10.1016/j.pestbp.2022.105084
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The insect-specific epsilon class of glutathione S-transferases (GSTEs) plays important roles in insecticide detoxification in insects. In our previous work, five GSTEs were identified in Locusta migratoria, and two recombinant GSTEs, rLmGSTE1 and rLmGSTE4, showed high catalytic activity when 1-chloro-2,4-dinitrobenzene (CDNB) was used as a substrate. In this work, we further investigated whether these two GSTEs could metabolize three insecticides including malathion, deltamethrin and DDT. Using ultra-high-performance liquid chromatography tandem mass spectrometry (UHPLC/MS) method, we found that rLmGSTE4, but not rLmGSTE1, can metabolize malathion and DDT. Malathion bioassays of L. migratoria after the expression of LmGSTE4 was suppressed by RNA interference (RNAi) showed increased insect mortality from 33.8% to 68.9%. However, no changes in mortality were observed in deltamethrin- or DDT-treated L. migratoria after the expression of LmGSTE4 was suppressed by RNAi. Our results provided direct evidences that LmGSTE4 participates in malathion detoxification in L. migratoria. These findings are important for understanding the mechanisms of insecticide resistance in L. migratoria and developing new strategies for managing the insect populations in the field.
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页数:9
相关论文
共 38 条
  • [1] [Anonymous], NYT27362015 AGR IND
  • [2] Aravindan V, 2014, J VECTOR DIS, V51, P8
  • [3] BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
  • [4] Autotransporter domain-dependent enzymatic analysis of a novel extremely thermostable carboxylesterase with high biodegradability towards pyrethroid pesticides
    Cai, Xianghai
    Wang, Wei
    Lin, Lin
    He, Dannong
    Huang, Gang
    Shen, Yaling
    Wei, Wei
    Wei, Dongzhi
    [J]. SCIENTIFIC REPORTS, 2017, 7
  • [5] Two epsilon glutathione S-transferase cDNAs from the common cutworm, Spodoptera litura: Characterization and developmental and induced expression by insecticides
    Deng, Huimin
    Huang, Yufen
    Feng, Qili
    Zheng, Sichun
    [J]. JOURNAL OF INSECT PHYSIOLOGY, 2009, 55 (12) : 1174 - 1183
  • [6] MUSCLE: multiple sequence alignment with high accuracy and high throughput
    Edgar, RC
    [J]. NUCLEIC ACIDS RESEARCH, 2004, 32 (05) : 1792 - 1797
  • [7] Insect glutathione transferases and insecticide resistance
    Enayati, AA
    Ranson, H
    Hemingway, J
    [J]. INSECT MOLECULAR BIOLOGY, 2005, 14 (01) : 3 - 8
  • [8] Resistance to commonly used insecticides and underlying mechanisms of resistance in Aedes aegypti (L.) from Sri Lanka
    Fernando, H. Sachini D.
    Saavedra-Rodriguez, Karla
    Perera, Rushika
    Black, William C.
    De Silva, B. G. D. Nissanka Kolitha
    [J]. PARASITES & VECTORS, 2020, 13 (01)
  • [9] Glutathione S-Transferase conjugation of organophosphorus pesticides yields S-Phospho-, S-Aryl-, and S-Alkylglutathione derivatives
    Fujioka, Kazutoshi
    Casida, John E.
    [J]. CHEMICAL RESEARCH IN TOXICOLOGY, 2007, 20 (08) : 1211 - 1217
  • [10] Gasteiger E., 2005, PROTEOMICS PROTOCOLS, P571, DOI [10.1385/1-59259-890-0:571, DOI 10.1385/1-59259-890-0:571]