Substrate specificity and promiscuity of horizontally transferred UDP-glycosyltransferases in the generalist herbivore Tetranychus urticae

Snoeck, Simon; Pavlidi, Nena; Pipini, Dimitra; Vontas, John; Dermauw, Wannes; Leeuwen, Thomas Van

doi:10.1016/j.ibmb.2019.04.010

Cited by 46 publications

(64 citation statements)

References 93 publications

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“…Our results are also consistent with previous research results on the role of UGTs in host adaptation in other phytophagous insects [17][18][19][20][21][22]. For example, nine UGT genes in three insects (HAUGT41B3 and HAUGT40D1 in H. armigera [16]; TUUGT204B2, TUUGT202A2, and TUUGT202A15 in T. urticae [11]; and UGT330A3, UGT344D5, UGT348A3, and UGT349A3 in Myzus persicae) [51] were associated with the detoxification of plant secondary metabolites, specifically gossypol, flavonoid and nicotine by the three insect species. As shown in Figure 3, UGT354A1 was closely related to subfamilies of APUGT330A, APUGT344D, APUGT348A, and APUGT349A.…”

Section: Discussionsupporting

confidence: 93%

“…In Helicoverpa armigera, UGT41B3 and UGT40D1 were found associated with detoxification of gossypol [16]. Snoeck et al reported that multiple compounds of the flavonoid class of plant secondary metabolites were glycosylated by three UGTs (tetur02g09850, tetur22g00270 and tetur22g00440) in T. urticae [11]. In additional, the expression profiles of T. urticae UGT genes changed after host-plant shifts [22].…”

Section: Introductionmentioning

confidence: 99%

“…Genome sequence and functional analyses have identified a variety of adaptation mechanisms in T. urticae, including expansion of genes coding for detoxification enzymes, such as cytochrome P450 monooxygenases, carboxyl-choline esterases, and glutathione-S-transferases, as well as a proliferation of cysteine peptidases, and MFS and ABC transporters [3][4][5][6]. In addition, T. urticae has a large repertoire of genes coding for uridine diphosphate (UDP)-glycosyltransferases (UGTs) and intradiol-ring cleavage dioxygenases [7][8][9][10][11]. Comparative analyses revealed that these genes in T. urticae were obtained through horizontal gene transfer but their expressions differed significantly depending on the specific host plants that they feed on [3,6,8,[12][13][14].…”

Section: Introductionmentioning

confidence: 99%

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Genome-Wide Identification and Expression Analysis of Udp-Glucuronosyltransferases in the Whitefly Bemisia Tabaci (Gennadius) (HemipterA: Aleyrodidae)

Guo

Xie

Yang

et al. 2020

IJMS

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Bemisia tabaci (Gennadius) (Hemiptera: Aleyrodidae) is an important agricultural pest worldwide. Uridine diphosphate (UDP)-glucuronosyltransferases (UGTs) are one of the largest and most ubiquitous groups of proteins. Because of their role in detoxification, insect UGTs are attracting increasing attention. In this study, we identified and analyzed UGT genes in B. tabaci MEAM1 to investigate their potential roles in host adaptation and reproductive capacity. Based on phylogenetic and structural analyses, we identified 76 UGT genes in the B. tabaci MEAM1 genome. RNA-seq and real-time quantitative PCR (RT-qPCR) revealed differential expression patterns of these genes at different developmental stages and in association with four host plants (cabbage, cucumber, cotton and tomato). RNA interference results of selected UGTs showed that, when UGT352A1, UGT352B1, and UGT354A1 were respectively silenced by feeding on dsRNA, the fecundity of B. tabaci MEAM1 was reduced, suggesting that the expressions of these three UGT genes in this species may be associated with host-related fecundity. Together, our results provide detailed UGTs data in B.tabaci and help guide future studies on the mechanisms of host adaptation by B.tabaci.

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Section: Discussionsupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Genome-Wide Identification and Expression Analysis of Udp-Glucuronosyltransferases in the Whitefly Bemisia Tabaci (Gennadius) (HemipterA: Aleyrodidae)

Guo

Xie

Yang

et al. 2020

IJMS

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“…Several studies have reported T. urticae strains with high levels of resistance against certain active ingredients, 22–25 including some cases of cross‐ or multiple resistance 18,26–28 . Several mechanisms have been associated with these phenotypes, with the most studied being target‐site mutations, 9,27,29–32 and over‐expression of detoxification enzymes 33–39 …”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of striking multiple‐insecticide resistance in a Tetranychus urticae field population from Greece

Papapostolou

Riga

Charamis

et al. 2020

Pest Management Science

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BACKGROUND Tetranychus urticae is a notorious crop pest with a worldwide distribution that has developed resistance to a wide range of acaricides. Here, we investigated the resistance levels of a T. urticae population collected from an ornamental greenhouse in Peloponnese, Greece, and analyzed its resistance mechanisms at the molecular level. RESULTS Toxicological assays showed resistance against compounds with different modes of action, with resistance ratios of: 89‐fold for abamectin; > 1000‐fold for clofentezine; > 5000‐fold for etoxazole; 27‐fold for fenpyroximate and pyridaben; 20‐ and 36‐fold for spirodiclofen and spirotetramat, respectively; and 116‐ and > 500‐fold for cyenopyrafen and cyflumetofen, respectively. Bioassays with synergists indicated the involvement of detoxification enzymes in resistance to abamectin, but not to cyflumetofen and spirodiclofen. RNA sequencing (RNA‐seq) analysis showed significant over‐expression of several genes encoding detoxification enzymes such as cytochrome P450 monooxygenases and UDP‐glycosyltransferases, which have been previously associated with acaricide resistance. Known target‐site resistance mutations were identified in acetyl‐choline esterase, chitin synthase 1 and NDUFS7/psst, but putative novel resistance mutations were also discovered in targets such as glutamate‐gated chloride channel subunit 3. Interestingly, target‐site resistance mutations against pyrethroids or bifenazate were not identified, possibly indicating a recent reduced selection pressure in Greece, as well as a possible opportunity to rotate these chemistries. CONCLUSION We identified and characterized a striking case of multiple acaricide resistance in a field population of T. urticae. Exceptionally strong resistance phenotypes, with accumulation of multiple resistance mutations and over‐expression of P450s and other detoxification genes in the same field population are reported.

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“…However, T. urticae has developed high levels of resistance to numerous acaricide compounds, due both to its biology (arrhenotokous reproduction, short life-cycle, and high fecundity) and to strong acaricide selection pressure [4,5]. Acaricide resistance in T. urticae has been associated with different mechanisms, including target-site mutations [6][7][8][9][10][11][12][13][14][15][16][17][18][19] and enhanced detoxification [20] through the overexpression of different classes of metabolic proteins, such as cytochrome P450s [17,19,[21][22][23][24], glutathione S-transferases [25,26], carboxylesterases [27], ABC transporters [28], and UDP-glycosyltransferases [17,29].…”

Section: Introductionmentioning

confidence: 99%

Co-Expression of a Homologous Cytochrome P450 Reductase Is Required for In Vivo Validation of the Tetranychus urticae CYP392A16-Based Abamectin Resistance in Drosophila

Riga

Ilias

Vontas

et al. 2020

Insects

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Overexpression of the cytochrome P450 monooxygenase CYP392A16 has been previously associated with abamectin resistance using transcriptional analysis in the two-spotted spider mite Tetranychus urticae, an important pest species worldwide; however, this association has not been functionally validated in vivo despite the demonstrated ability of CYP392A16 to metabolize abamectin in vitro. We expressed CYP392A16 in vivo via a Gal4 transcription activator protein/Upstream Activating Sequence (GAL4/UAS) system in Drosophila melanogaster flies, driving expression with detoxification tissue-specific drivers. We demonstrated that CYP392A16 expression confers statistically significant abamectin resistance in toxicity bioassays in Drosophila only when its homologous redox partner, cytochrome P450 reductase (TuCPR), is co-expressed in transgenic flies. Our study shows that the Drosophila model can be further improved, to facilitate the functional analysis of insecticide resistance mechanisms acting alone or in combination.

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Substrate specificity and promiscuity of horizontally transferred UDP-glycosyltransferases in the generalist herbivore Tetranychus urticae

Cited by 46 publications

References 93 publications

Genome-Wide Identification and Expression Analysis of Udp-Glucuronosyltransferases in the Whitefly Bemisia Tabaci (Gennadius) (HemipterA: Aleyrodidae)

Genome-Wide Identification and Expression Analysis of Udp-Glucuronosyltransferases in the Whitefly Bemisia Tabaci (Gennadius) (HemipterA: Aleyrodidae)

Identification and characterization of striking multiple‐insecticide resistance in a Tetranychus urticae field population from Greece

Co-Expression of a Homologous Cytochrome P450 Reductase Is Required for In Vivo Validation of the Tetranychus urticae CYP392A16-Based Abamectin Resistance in Drosophila

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