Identification of an alternative knockdown resistance (<i>kdr</i>)-like mutation, M918L, and a novel mutation, V1010A, in the<i>Thrips tabaci</i>voltage-gated sodium channel gene

Wu, Minchen; Gotoh, Hiroki; Waters, Timothy D.; Walsh, Douglas B.; Lavine, Laura Corley

doi:10.1002/ps.3638

Cited by 25 publications

(15 citation statements)

References 34 publications

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“…Mutations located in these regions, either alone or in combination with others, have been associated with high (super-kdr) levels of resistance to pyrethroids in many arthropod species (Dong et al, 2014). The M918L and L925V mutations identified in this study, that map to domain II, have been described previously in Aphis gossypii (Glover) (Hemiptera: Aphididae) (Carletto et al, 2010), Myzus persicae (Sulzer) (Hemiptera: Aphididae) (Panini et al, 2015), Hyalella azteca (Saussure) (Amphipoda: Hyalellidae) (Weston et al, 2013), Trialeurodes vaporariorum Westwood (Hemiptera: Aleyrodidae) (Karatolos et al, 2012) and Thrips tabaci Lindeman (Thysanoptera: Thripidae) (Wu et al, 2014) and V. destructor (González-Cabrera et al, 2013). However, those mapping to domain IIIS6 (A1536T and S1539T) have not previously been identified as associated with resistance.…”

Section: Discussionsupporting

confidence: 67%

Mutations in the voltage‐gated sodium channel gene associated with deltamethrin resistance in commercially sourced Phytoseiulus persimilis

Benavent‐Albarracín

Alonso

Catalán

et al. 2020

Insect Molecular Biology

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The implementation of Integrated Pest Management (IPM) in current agricultural practice is a convenient and very effective strategy to maintain pest populations under control. The use of biological control agents, like Phytoseiulus persimilis, is key for the success of such an approach. This predatory mite is widely used since it is very effective for controlling Tetranychus urticae, one of the most devastating crop pests.Here we identify several mutations located in the Voltage Gated Sodium Channel (VGSC) of commercially sourced P. persimilis that correlate with a reduced susceptibility to the pyrethroid deltamethrin. We found that the mites sourced from two different biocontrol product companies have intrinsic genotypic differences that correlate with their phenotype when tested with different concentrations of deltamethrin. Mites from Syngenta Bioline, carrying the mutations M918L and A1536T, were able to survive deltamethrin concentrations of up to 10 ppm, while the mites from Koppert Biological Systems, with the combination M918L, L925V and S1539T, survived treatment with 40 ppm. All of the point mutations identified in the predatory mite samples are located in a particular region of the VGSC, previously proposed as the binding site for this family of pesticides and identified as a 'hot spot' for resistance.

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Section: Discussionsupporting

confidence: 67%

Mutations in the voltage‐gated sodium channel gene associated with deltamethrin resistance in commercially sourced Phytoseiulus persimilis

Benavent‐Albarracín

Alonso

Catalán

et al. 2020

Insect Molecular Biology

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“…Due to its essential role in electrical signaling, VGSC is the target of several neurotoxins, including pyrethroids and DDT 34 . Many amino acid substitutions associated with pyrethroid resistance in arthropods are located in transmembrane segments 4–6 of domain II (IIS4-IIS6) including M918 (super kdr ), L925, T929, L932, V1010, L1014 ( kdr ), and L1024 30 34 35 36 . One mutation within the intracellular inter linker connecting domains II and III (A1215D) and one mutation in domain III (F1538I) were detected in a highly bifenthrin resistant T. urticae strain from Greece 29 .…”

Section: Resultsmentioning

confidence: 99%

“…Because of their safety, longevity of residual activity and low cost, pyrethroids are extensively used for pest control, with about a 20% insecticide market share 23 . Unfortunately, ubiquitous resistance to pyrethroids had been broadly reported in various insect populations 19 20 34 36 54 . In T. urticae , two mutations, F1538I in domain IIIS6 and A1215D within the intracellular inter linker connecting domains II and III were linked with high bifenthrin resistance in a Greek population 29 .…”

Section: Discussionmentioning

confidence: 99%

Molecular mechanisms of Tetranychus urticae chemical adaptation in hop fields

Piraneo

Bull

Morales

et al. 2015

Sci Rep

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The two-spotted spider mite, Tetranychus urticae Koch is a major pest that feeds on >1,100 plant species. Many perennial crops including hop (Humulus lupulus) are routinely plagued by T. urticae infestations. Hop is a specialty crop in Pacific Northwest states, where 99% of all U.S. hops are produced. To suppress T. urticae, growers often apply various acaricides. Unfortunately T. urticae has been documented to quickly develop resistance to these acaricides which directly cause control failures. Here, we investigated resistance ratios and distribution of multiple resistance-associated mutations in field collected T. urticae samples compared with a susceptible population. Our research revealed that a mutation in the cytochrome b gene (G126S) in 35% tested T. urticae populations and a mutation in the voltage-gated sodium channel gene (F1538I) in 66.7% populations may contribute resistance to bifenazate and bifenthrin, respectively. No mutations were detected in Glutamate-gated chloride channel subunits tested, suggesting target site insensitivity may not be important in our hop T. urticae resistance to abamectin. However, P450-mediated detoxification was observed and is a putative mechanism for abamectin resistance. Molecular mechanisms of T. urticae chemical adaptation in hopyards is imperative new information that will help growers develop effective and sustainable management strategies.

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“…We are not aware of alanine substitutions of these residues, but substitutions T 2o10 I or I 1o10 C by bigger residues decrease the ligands potency (Table 1), which may be explained in our models of PyR1 and PyR2 by a more restricted access path for pyrethroids from the membrane to their receptors. V 2i12 A and V 2i12 L are putative kdr mutations in PyR2, which are found to coexist with kdr mutations M 2k11 L and L 2i16 S in pyrethroid-resistant populations of Thrips tabaci (Wu et al, 2014) and Anopheles culicifacies (Singh et al, 2010). Importantly, M 2k11 L and L 2i16 S significantly reduce channel sensitivity to pyrethroids (Table 1), and we suggest that the double mutations may have synergistic effects due to decreasing the ligand-channel interactions and facilitating the ligand egress from PyR1 and PyR2.…”

Section: Symmetry Of Two Pyrethroid Receptorsmentioning

confidence: 99%

Rotational Symmetry of Two Pyrethroid Receptor Sites in the Mosquito Sodium Channel

Nomura

Zhorov

et al. 2015

Mol Pharmacol

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Voltage-gated sodium channels are the primary target of pyrethroid insecticides. Although it is well known that specific mutations in insect sodium channels confer knockdown resistance (kdr) to pyrethroids, the atomic mechanisms of pyrethroid-sodium channel interactions are not clearly understood. Previously, computer modeling and mutational analysis predicted two pyrethroid receptors, pyrethroid receptor site 1 (PyR1) (initial) and pyrethroid receptor site 2 (PyR2), located in the domain interfaces II/III and I/II, respectively. The models differ in ligand orientation and the number of transmembrane helices involved. In this study, we elaborated a revised PyR1 model of the mosquito sodium channel. Computational docking in the K v 1.2-based open channel model yielded a complex in which a pyrethroid (deltamethrin) binds between the linker helix IIL45 and transmembrane helices IIS5, IIS6, and IIIS6 with its dibromoethenyl and diphenylether moieties oriented in the intra-and extracellular directions, respectively. The PyR2 and revised PyR1 models explained recently discovered kdr mutations and predicted new deltamethrin-channel contacts. Further model-driven mutagenesis identified seven new pyrethroid-sensing residues, three in the revised PyR1 and four in PyR2. Our data support the following conclusions: 1) each pyrethroid receptor is formed by a linker-helix L45 and three transmembrane helices (S5 and two S6s); 2) IIS6 contains four residues that contribute to PyR1 and another four to PyR2; 3) seven pairs of pyrethroid-sensing residues are located in symmetric positions within PyR1 and PyR2; and 4) pyrethroids bind to PyR1 and PyR2 in similar orientations, penetrating deeply into the respective domain interfaces. Our study elaborates the dual pyrethroid-receptor sites concept and provides a structural background for rational development of new insecticides.

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Identification of an alternative knockdown resistance (kdr)-like mutation, M918L, and a novel mutation, V1010A, in theThrips tabacivoltage-gated sodium channel gene

Cited by 25 publications

References 34 publications

Mutations in the voltage‐gated sodium channel gene associated with deltamethrin resistance in commercially sourced Phytoseiulus persimilis

Mutations in the voltage‐gated sodium channel gene associated with deltamethrin resistance in commercially sourced Phytoseiulus persimilis

Molecular mechanisms of Tetranychus urticae chemical adaptation in hop fields

Rotational Symmetry of Two Pyrethroid Receptor Sites in the Mosquito Sodium Channel

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