Functional characterization of glutathione S-transferases associated with insecticide resistance in Tetranychus urticae

Pavlidi, Nena; Tseliou, Vasilis; Riga, Maria; Nauen, Ralf; Leeuwen, Thomas Van; Labrou, Nikolaos E.; Vontas, John

doi:10.1016/j.pestbp.2015.01.009

Cited by 74 publications

(82 citation statements)

References 30 publications

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“…Glutathione S‐transferase (GSTs) is one of important detoxification enzymes, which can catalyze GSH conjugating with chemicals to increase their hydrophilism and to facilitate its excretion from the cell in animals insects and mites . GSTs have contributed to kinds of insecticides or acaricides' resistance by direct or indirect metabolism of chemicals in insects and mites, such as dehydrochlorination of organochlorines by GSTs catalyzed in Anopheles gambiae and catalyzed GSH binding with abamectin by TuGSTd14 in T. urticae . On the other hand, a single mutation L119F in an upregulated GST gene, GSTe2, also conferred high resistance to DDT in Anopheles funestus .…”

Section: Introductionsupporting

confidence: 54%

Stability of cyflumetofen resistance in Tetranychus cinnabarinus and its correlation with glutathione‐S‐transferase gene expression

Feng

Yang

Wen

et al. 2019

Pest Management Science

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BACKGROUND Cyflumetofen is an outstanding acaricide with a novel mode of action. Tetranychus cinnabarinus, an important agricultural pest, is notorious for developing resistance to most classes of acaricides rapidly and results in enormous loss for the economy. Our previous study had pointed out glutathione S‐transferase (GSTs) significantly contributed to the cyflumetofen‐resistance formation in T. cinnabarinus, but the more specific mechanism needed to be further investigated. RESULTS The unstable resistance was observed in cyflumetofen‐resistant strain (CyR)under acaricide‐free condition. The activity of GSTs increased along with the development of resistance. The expressions of 13 GST genes were detected in CyR and susceptible strain (SS), of which six genes were overexpressed in CyR and the TcGSTm02 was selected as the representative for functional study. The expression of TcGSTm02 changed along with the resistant level of CyR with the same trend. Recombinant protein of TcGSTm02 with high activity was successfully obtained by E. coli expression system, whose activity could be inhibited by cyflumetofen (IC50 = 0.23 mM). Recombinant TcGSTm02 could effectively decompose cyflumetofen, and catalyze GS− to conjugate with cyflumetofen. CONCLUSION All clues confirmed that GSTs strongly associated with cyflumetofen‐resistance and a representative gene, TcGSTm02, showed function on contributing the evolution of cyflumetofen‐resistance in T. cinnabarinus. © 2019 Society of Chemical Industry

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Section: Introductionsupporting

confidence: 54%

Stability of cyflumetofen resistance in Tetranychus cinnabarinus and its correlation with glutathione‐S‐transferase gene expression

Feng

Yang

Wen

et al. 2019

Pest Management Science

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“…This might result in the V max and K m values of BdGSTd10 being higher than BdGSTd1. GSTs can interact with, or be inhibited by, hexythiazox, cyflumetofen, pyridaben, bifenthrin, abamectin, and clofentezine in Tetranychus urticae . However, knowledge of malathion inhibition of GSTs activity in B. dorsalis is meager.…”

Section: Discussionmentioning

confidence: 99%

Two delta class glutathione S‐transferases involved in the detoxification of malathion in Bactrocera dorsalis (Hendel)

Meng

Yuan

et al. 2019

Pest Management Science

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BACKGROUND The oriental fruit fly Bactrocera dorsalis (Hendel), a widespread agricultural pest, has evolved resistance to many insecticides, including organophosphorus compounds. Glutathione S‐transferases (GSTs) are involved in xenobiotic detoxification and insecticide resistance in many insects. However, the role of delta class GSTs in detoxifying malathion in B. dorsalis is unknown. Here, we evaluated the roles of two delta class GSTs in malathion detoxification in this species. RESULTS Two delta class GSTs genes, BdGSTd1 and BdGSTd10, were characterized in B. dorsalis. They were highly expressed in 5‐day‐old adults, as well as in midgut and Malpighian tubules. Upon malathion exposure, the two genes were upregulated by 2.63‐ and 2.85‐fold, respectively. Injection of double‐stranded RNA targeting BdGSTd1 or BdGSTd10 significantly reduced their mRNA levels in adults and also significantly increased adult susceptibility to malathion. The expression of these two GSTs in Escherichia coli helped the host to endure malathion stress at a concentration of 10 µg mL−1 according to a Cell Counting Kit‐8 assay. High‐performance liquid chromatography analyses indicated that malathion could be significantly depleted by the two delta GSTs. The role of BdGSTd10 in malathion sequestration was also discussed. CONCLUSION BdGSTd1 and BdGSTd10 play important roles in the detoxification of malathion in B. dorsalis. © 2019 Society of Chemical Industry

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“…Reports of abamectin/milbemectin field resistance remain relatively scarce for T. urticae , despite the heavy use of both compounds against spider mite infestations for more than 30 years (Campos, Dybas, & Krupa, 1995; Campos, Krupa, & Dybas, 1996; Kwon, Lee, Ahn, & Lee, 2014; Stumpf & Nauen, 2002; Van Leeuwen et al., 2010). Abamectin resistance is known to evolve through different mechanisms and can include target‐site and/or biochemical/metabolic resistance (Dermauw et al., 2012; Kwon, Yoon, et al., 2010; Pavlidi et al., 2015; Riga et al., 2014, 2017). Previous studies have however shown that target‐site resistance is only of minor importance for the occasionally encountered high resistance levels in field populations (Riga et al., 2017).…”

Section: Discussionmentioning

confidence: 99%

“…A combination of the two GluCl mutations does not confer high resistance levels to abamectin in T. urticae (Riga et al., 2017) and may thus act as a resistance limiting factor, maintaining a high efficiency of abamectin, regardless of its long history of use (Pavlidi et al., 2015; Riga et al., 2014). This scenario finds its support in the worldwide survey by Ilias et al.…”

Section: Discussionmentioning

confidence: 99%

Fitness costs of key point mutations that underlie acaricide target‐site resistance in the two‐spotted spider mite Tetranychus urticae

Bajda

Riga

Wybouw

et al. 2018

Evolutionary Applications

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The frequency of insecticide/acaricide target‐site resistance is increasing in arthropod pest populations and is typically underpinned by single point mutations that affect the binding strength between the insecticide/acaricide and its target‐site. Theory predicts that although resistance mutations clearly have advantageous effects under the selection pressure of the insecticide/acaricide, they might convey negative pleiotropic effects on other aspects of fitness. If such fitness costs are in place, target‐site resistance is thus likely to disappear in the absence of insecticide/acaricide treatment, a process that would counteract the spread of resistance in agricultural crops. Hence, there is a great need to reliably quantify the various potential pleiotropic effects of target‐site resistance point mutations on arthropod fitness. Here, we used near‐isogenic lines of the spider mite pest Tetranychus urticae that carry well‐characterized acaricide target‐site resistance mutations to quantify potential fitness costs. Specifically, we analyzed P262T in the mitochondrial cytochrome b, the combined G314D and G326E substitutions in the glutamate‐gated chloride channels, L1024V in the voltage‐gated sodium channel, and I1017F in chitin synthase 1. Five fertility life table parameters and nine single‐generation life‐history traits were quantified and compared across a total of 15 mite lines. In addition, we monitored the temporal resistance level dynamics of populations with different starting frequency levels of the chitin synthase resistant allele to further support our findings. Three target‐site resistance mutations, I1017F and the co‐occurring G314D and G326E mutations, were shown to significantly and consistently alter certain fitness parameters in T. urticae. The other two mutations (P262T and L1024V) did not result in any consistent change in a fitness parameter analyzed in our study. Our findings are discussed in the context of the global spread of T. urticae pesticide resistance and integrated pest management.

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Functional characterization of glutathione S-transferases associated with insecticide resistance in Tetranychus urticae

Cited by 74 publications

References 30 publications

Stability of cyflumetofen resistance in Tetranychus cinnabarinus and its correlation with glutathione‐S‐transferase gene expression

Stability of cyflumetofen resistance in Tetranychus cinnabarinus and its correlation with glutathione‐S‐transferase gene expression

Two delta class glutathione S‐transferases involved in the detoxification of malathion in Bactrocera dorsalis (Hendel)

Fitness costs of key point mutations that underlie acaricide target‐site resistance in the two‐spotted spider mite Tetranychus urticae

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