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

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  • POLYADAPT (Molecular-genetic mechanisms of extreme adaptation in a polyphagous agricultural pest)
  • SuperPests (Innovative tools for rational control of the most difficult-to-manage pests (super pests) and the diseases they transmit)
Abstract
Uridine diphosphate (UDP)-glycosyltransferases (UGTs) catalyze the addition of UDP-sugars to small hydrophobic molecules, turning them into more water-soluble metabolites. While their role in detoxification is well documented for vertebrates, arthropod UGTs have only recently been linked to the detoxification and sequestration of plant toxins and insecticides. The two-spotted spider mite Tetranychus urticae is a generalist herbivore notorious for rapidly developing resistance to insecticides and acaricides. We identified a set of eight UGT genes that were overexpressed in mites upon long-term acclimation or adaptation to a new host plant and/or in mite strains highly resistant to acaricides. Functional expression revealed that they were all catalytically active and that the majority preferred UDP-glucose as activated donor for glycosylation of model substrates. A high-throughput substrate screening of both plant secondary metabolites and pesticides revealed patterns of both substrate specificity and promiscuity. We further selected nine enzyme-substrate combinations for more comprehensive analysis and determined steady-state kinetic parameters. Among others, plant metabolites such as capsaicin and several flavonoids were shown to be glycosylated. The acaricide abamectin was also glycosylated by two UGTs and one of these was also overexpressed in an abamectin resistant strain. Our study corroborates the potential role of T. urticae UGTs in detoxification of both synthetic and natural xenobiotic compounds and paves the way for rapid substrate screening of arthropod UGTs.
Keywords
2-SPOTTED SPIDER-MITE, INSECTICIDE RESISTANCE, ACARICIDE RESISTANCE, ABAMECTIN RESISTANCE, METABOLIC RESISTANCE, MOLECULAR ANALYSIS, HYDROXAMIC ACIDS, DETOXIFICATION, MECHANISMS, GLYCOSYLATION

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Citation

Please use this url to cite or link to this publication:

MLA
Snoeck, Simon, et al. “Substrate Specificity and Promiscuity of Horizontally Transferred UDP-Glycosyltransferases in the Generalist Herbivore Tetranychus Urticae.” INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, vol. 109, 2019, pp. 116–27.
APA
Snoeck, S., Pavlidi, N., Pipini, D., Vontas, J., Dermauw, W., & Van Leeuwen, T. (2019). Substrate specificity and promiscuity of horizontally transferred UDP-glycosyltransferases in the generalist herbivore Tetranychus urticae. INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, 109, 116–127.
Chicago author-date
Snoeck, Simon, Nena Pavlidi, Dimitra Pipini, John Vontas, Wannes Dermauw, and Thomas Van Leeuwen. 2019. “Substrate Specificity and Promiscuity of Horizontally Transferred UDP-Glycosyltransferases in the Generalist Herbivore Tetranychus Urticae.” INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY 109: 116–27.
Chicago author-date (all authors)
Snoeck, Simon, Nena Pavlidi, Dimitra Pipini, John Vontas, Wannes Dermauw, and Thomas Van Leeuwen. 2019. “Substrate Specificity and Promiscuity of Horizontally Transferred UDP-Glycosyltransferases in the Generalist Herbivore Tetranychus Urticae.” INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY 109: 116–127.
Vancouver
1.
Snoeck S, Pavlidi N, Pipini D, Vontas J, Dermauw W, Van Leeuwen T. Substrate specificity and promiscuity of horizontally transferred UDP-glycosyltransferases in the generalist herbivore Tetranychus urticae. INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY. 2019;109:116–27.
IEEE
[1]
S. Snoeck, N. Pavlidi, D. Pipini, J. Vontas, W. Dermauw, and T. Van Leeuwen, “Substrate specificity and promiscuity of horizontally transferred UDP-glycosyltransferases in the generalist herbivore Tetranychus urticae,” INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, vol. 109, pp. 116–127, 2019.
@article{8614450,
  abstract     = {Uridine diphosphate (UDP)-glycosyltransferases (UGTs) catalyze the addition of UDP-sugars to small hydrophobic molecules, turning them into more water-soluble metabolites. While their role in detoxification is well documented for vertebrates, arthropod UGTs have only recently been linked to the detoxification and sequestration of plant toxins and insecticides. The two-spotted spider mite Tetranychus urticae is a generalist herbivore notorious for rapidly developing resistance to insecticides and acaricides. We identified a set of eight UGT genes that were overexpressed in mites upon long-term acclimation or adaptation to a new host plant and/or in mite strains highly resistant to acaricides. Functional expression revealed that they were all catalytically active and that the majority preferred UDP-glucose as activated donor for glycosylation of model substrates. A high-throughput substrate screening of both plant secondary metabolites and pesticides revealed patterns of both substrate specificity and promiscuity. We further selected nine enzyme-substrate combinations for more comprehensive analysis and determined steady-state kinetic parameters. Among others, plant metabolites such as capsaicin and several flavonoids were shown to be glycosylated. The acaricide abamectin was also glycosylated by two UGTs and one of these was also overexpressed in an abamectin resistant strain. Our study corroborates the potential role of T. urticae UGTs in detoxification of both synthetic and natural xenobiotic compounds and paves the way for rapid substrate screening of arthropod UGTs.},
  author       = {Snoeck, Simon and Pavlidi, Nena and Pipini, Dimitra and Vontas, John and Dermauw, Wannes and Van Leeuwen, Thomas},
  issn         = {0965-1748},
  journal      = {INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY},
  keywords     = {2-SPOTTED SPIDER-MITE,INSECTICIDE RESISTANCE,ACARICIDE RESISTANCE,ABAMECTIN RESISTANCE,METABOLIC RESISTANCE,MOLECULAR ANALYSIS,HYDROXAMIC ACIDS,DETOXIFICATION,MECHANISMS,GLYCOSYLATION},
  language     = {eng},
  pages        = {116--127},
  title        = {Substrate specificity and promiscuity of horizontally transferred UDP-glycosyltransferases in the generalist herbivore Tetranychus urticae},
  url          = {http://dx.doi.org/10.1016/j.ibmb.2019.04.010},
  volume       = {109},
  year         = {2019},
}

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