Identification and Characterization of Glutathione S-Transferase Genes in the Antennae of Codling Moth (Lepidoptera: Tortricidae)

Huang, Xinglong; Fan, Dongsheng; Liu, Lu; Feng, Jinian

doi:10.1093/aesa/sax041

Cited by 28 publications

(41 citation statements)

References 35 publications

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“…As seen previously, SlitGSTd2 clusters in a conserved subgroup which includes BmGSTd4 and CpomGSTd2 for which predicted signal peptide (SP) sequences have been identified (Tan et al, 2014; Huang et al, 2017). SlitGSTd2 possesses also a predicted 22 amino acid SP at the N-terminus of the protein sequence, and its presence was confirmed by using RT-PCR with specific primers (Figure S1).…”

Section: Resultsmentioning

confidence: 79%

“…Moreover, all the delta GSTs from moths known to have an antennal specific expression, such as MsexGST-msolf from M. sexta (Robertson et al, 1999; Rogers et al, 1999), BmGSTd4 from B. mori (Tan et al, 2014), GST-haolf (Wang et al, 2004) from H. armigera and CpomGSTd2 (Huang et al, 2017) from C. pomonella fall within this clade.…”

Section: Resultsmentioning

confidence: 99%

“…However, as far as expression information is available, the second one with SlitGSTd2 is only composed of antennal-specific enzymes, such as B. mori, M. sexta , and A. transitella and C. pomonella GSTs (Rogers et al, 1999; Leal et al, 2009; Tan et al, 2014; Huang et al, 2017). MsexGST-msolf has been shown to degrade odorants in vitro and may have a role of ODE, especially toward aldehyde odorants, whereas CpomGSTd2 is active toward insecticides.…”

Section: Discussionmentioning

confidence: 99%

“…However, the expression of GSTs as well as their activities have been also highlighted in the olfactory organs of several insect species. Antennal expressed GSTs have been indeed identified in various moth species, such as Manduca sexta (Rogers et al, 1999), Helicoverpa armigera (Wang et al, 2004), Amyelois transitella (Leal et al, 2009), Bombyx mori (Tan et al, 2014), Chilo suppressalis (Liu et al, 2015a), Epiphyas postvittana (Corcoran et al, 2015), Cnaphalocris medinalis (Liu et al, 2015b), and Cydia pomonella (Huang et al, 2017), but also in the fruit fly Drosophila melanogaster (Younus et al, 2014) or in the beetles Agrilus planipennis (Mamidala et al, 2013), Dendroctonus valens (Gu et al, 2015), and Phyllotreta striolata (Wu et al, 2016). This particular localization led to the hypothesis of a possible dual function of GSTs in antennae where, besides their original implication in xenobiotic metabolism, they could play a role in the signal termination and in odorant clearance, as Odorant-Degrading Enzymes (ODEs, Vogt and Riddiford, 1981; Chertemps, 2017).…”

Section: Introductionmentioning

confidence: 99%

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Glutathione-S-Transferases in the Olfactory Organ of the Noctuid Moth Spodoptera littoralis, Diversity and Conservation of Chemosensory Clades

et al. 2018

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Glutathione-S-transferases (GSTs) are conjugating enzymes involved in the detoxification of a wide range of xenobiotic compounds. The expression of GSTs as well as their activities have been also highlighted in the olfactory organs of several species, including insects, where they could play a role in the signal termination and in odorant clearance. Using a transcriptomic approach, we identified 33 putative GSTs expressed in the antennae of the cotton leafworm Spodoptera littoralis. We established their expression patterns and revealed four olfactory-enriched genes in adults. In order to investigate the evolution of antennal GST repertoires in moths, we re-annotated antennal transcripts corresponding to GSTs in two moth and one coleopteran species. We performed a large phylogenetic analysis that revealed an unsuspected structural—and potentially functional—diversity of GSTs within the olfactory organ of insects. This led us to identify a conserved clade containing most of the already identified antennal-specific and antennal-enriched GSTs from moths. In addition, for all the sequences from this clade, we were able to identify a signal peptide, which is an unusual structural feature for GSTs. Taken together, these data highlight the diversity and evolution of GSTs in the olfactory organ of a pest species and more generally in the olfactory system of moths, and also the conservation of putative extracellular members across multiple insect orders.

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Section: Resultsmentioning

confidence: 79%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Glutathione-S-Transferases in the Olfactory Organ of the Noctuid Moth Spodoptera littoralis, Diversity and Conservation of Chemosensory Clades

et al. 2018

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“…Recombinant CpGSTd1 and CpGSTd3 enzymes have been shown to be indirectly involved in the metabolism of λ‐cyhalothrin . Insecticides β‐cyfluthrin, chlorpyrifos, thimet, and chlorbenzuron used for C. pomonella control were found to be able to inhibit the enzymatic activity of recombinant CpGSTd2 . Although increased C. pomonella GSTs activity has been linked with λ‐cyhalothrin resistance on several occasions and the potential roles of some specific GST genes in detoxification of λ‐cyhalothrin have been documented, systematic characterization of GSTs in the delta and epsilon subclasses in C. pomonella is currently still lacking.…”

Section: Introductionmentioning

confidence: 99%

Functional characterization of a novel λ‐cyhalothrin metabolizing glutathione S‐transferase, CpGSTe3, from the codling moth Cydia pomonella

Wang

et al. 2019

Pest Management Science

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BACKGROUND Recent work has shown that two codling moth (Cydia pomonella) glutathione S‐transferase genes (GSTs), CpGSTd1 and CpGSTd3, can metabolize λ‐cyhalothrin, one of the recommended insecticides for C. pomonella control worldwide. However, systematical characterization of delta and epsilon GSTs, especially their potential contributions in the metabolism of λ‐cyhalothrin, is currently still lacking in C. pomonella. RESULTS In this study, a total of nine cDNA sequences were identified in C. pomonella, including four in the delta and five in the epsilon subclasses. RT‐qPCR showed that seven GSTs were ubiquitously expressed at all developmental stages, and CpGSTe2, CpGSTe3, and CpGSTe4 were mainly expressed in larvae. The mRNA levels of CpGSTd2, CpGSTd4, and CpGSTe5 were significantly higher in male than in female adults. Tissue‐specific expression analysis revealed that the CpGSTe2, CpGSTe3, and CpGSTe4 were highly expressed in the midgut while CpGSTd2 and CpGSTd4 were predominantly expressed in the Malpighian tubules. The transcripts of these GSTs (except CpGSTe1) were co‐expressed following exposure to LD10 of λ‐cyhalothrin for 3 h. Recombinant CpGSTd4, CpGSTe2, and CpGSTe3 proteins expressed in Escherichia coli displayed glutathione‐conjugating activity toward 1‐chloro‐2,4‐dinitrobenzene. In addition, λ‐cyhalothrin could inhibit the activity of recombinant CpGSTd4, CpGSTe2, and CpGSTe3 enzymes, but only recombinant CpGSTe3 showed λ‐cyhalothrin metabolic capacity, with 21.88 ± 1.09% of parental compound being depleted within 1 h. CONCLUSION These data show that CpGSTe3 is a third GST gene, encoding an enzyme that metabolizes λ‐cyhalothrin in C. pomonella. © 2019 Society of Chemical Industry

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Structure–activity analysis suggests an olfactory function for the unique antennal delta glutathione transferase of Apis mellifera

Schwartz,

Boichot,

Muradova

et al. 2023

FEBS Letters

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Glutathione transferases (GST) are detoxification enzymes that conjugate glutathione to a wide array of molecules. In the honey bee Apis mellifera, AmGSTD1 is the sole member of the delta class of GSTs, with expression in antennae. Here, we structurally and biochemically characterized AmGSTD1 to elucidate its function. We showed that AmGSTD1 can efficiently catalyse the glutathione conjugation of classical GST substrates. Additionally, AmGSTD1 exhibits binding properties with a range of odorant compounds. AmGSTD1 has a peculiar interface with a structural motif we propose to call ‘sulfur sandwich’. This motif consists of a cysteine disulfide bridge sandwiched between the sulfur atoms of two methionine residues and is stabilized by CH…S hydrogen bonds and S…S sigma‐hole interactions. Thermal stability studies confirmed that this motif is important for AmGSTD1 stability and, thus, could facilitate its functions in olfaction.

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Identification and Characterization of Glutathione S-Transferase Genes in the Antennae of Codling Moth (Lepidoptera: Tortricidae)

Cited by 28 publications

References 35 publications

Glutathione-S-Transferases in the Olfactory Organ of the Noctuid Moth Spodoptera littoralis, Diversity and Conservation of Chemosensory Clades

Glutathione-S-Transferases in the Olfactory Organ of the Noctuid Moth Spodoptera littoralis, Diversity and Conservation of Chemosensory Clades

Functional characterization of a novel λ‐cyhalothrin metabolizing glutathione S‐transferase, CpGSTe3, from the codling moth Cydia pomonella

Structure–activity analysis suggests an olfactory function for the unique antennal delta glutathione transferase of Apis mellifera

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