Biochemical characterization of an unclassified glutathione &lt;i&gt;S&lt;/i&gt;-transferase of &lt;i&gt;Plutella xylostella&lt;/i&gt;

Yamamoto, Kohji; Hirowatari, Aiko; Shiotsuki, Takahiro; Yamada, Naotaka

doi:10.1584/jpestics.d16-048

Cited by 7 publications

(6 citation statements)

References 28 publications

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“…In our study, neither HNE nor T2H were conjugated to GSH enzymatically by LdGSTu1 ( Table 2 ). This result is consistent with bmGSTu2 and pxGSTu1, unclassified GSTs identified in silkworm [ 47 ] and diamondback moth [ 52 ], respectively.…”

Section: Discussionsupporting

confidence: 88%

Structural and Functional Characterization of One Unclassified Glutathione S-Transferase in Xenobiotic Adaptation of Leptinotarsa decemlineata

Liu

Moural

et al. 2021

IJMS

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Arthropod Glutathione S-transferases (GSTs) constitute a large family of multifunctional enzymes that are mainly associated with xenobiotic or stress adaptation. GST-mediated xenobiotic adaptation takes place through direct metabolism or sequestration of xenobiotics, and/or indirectly by providing protection against oxidative stress induced by xenobiotic exposure. To date, the roles of GSTs in xenobiotic adaptation in the Colorado potato beetle (CPB), a notorious agricultural pest of plants within Solanaceae, have not been well studied. Here, we functionally expressed and characterized an unclassified-class GST, LdGSTu1. The three-dimensional structure of the LdGSTu1 was solved with a resolution up to 1.8 Å by X-ray crystallography. The signature motif VSDGPPSL was identified in the “G-site”, and it contains the catalytically active residue Ser14. Recombinant LdGSTu1 was used to determine enzyme activity and kinetic parameters using 1-chloro-2, 4-dinitrobenzene (CDNB), GSH, p-nitrophenyl acetate (PNA) as substrates. The enzyme kinetic parameters and enzyme-substrate interaction studies demonstrated that LdGSTu1 could catalyze the conjugation of GSH to both CDNB and PNA, with a higher turnover number for CDNB than PNA. The LdGSTu1 enzyme inhibition assays demonstrated that the enzymatic conjugation of GSH to CDNB was inhibited by multiple pesticides, suggesting a potential function of LdGSTu1 in xenobiotic adaptation.

show abstract

Section: Discussionsupporting

confidence: 88%

Structural and Functional Characterization of One Unclassified Glutathione S-Transferase in Xenobiotic Adaptation of Leptinotarsa decemlineata

Liu

Moural

et al. 2021

IJMS

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show abstract

“…In our study, neither HNE nor T2H were conjugated to GSH enzymatically by LdGSTu1 (Table 2). This result is consistent with bmGSTu2 and pxGSTu1, unclassified GSTs identified in silkworm [63] and diamondback moth [68], respectively.…”

Section: Discussionsupporting

confidence: 87%

Structure and function of one unclassified-class glutathioneS-transferase inLeptinotarsa decemlineata

Liu

Moural

Koirala

et al. 2021

Preprint

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Arthropod Glutathione S-transferases (GSTs) constitute a large family of multifunctional enzymes that are mainly associated with xenobiotic or stress adaptation. GST-mediated xenobiotic adaptation is through direct metabolism or sequestration of xenobiotics, and/or indirectly by providing protection against oxidative stress induced by xenobiotic exposure. To date, the roles of GSTs in xenobiotic adaptation in the Colorado potato beetle (CPB), a notorious agriculture pest of plants within Solanaceae have not been well studied. Here, we functionally expressed and characterized an unclassified-class GST, LdGSTu1. The three-dimensional structure of the LdGSTu1 was solved with a resolution up to 1.8 Å by x-ray crystallography. Recombinant LdGSTu1 was used to determine enzyme activity and kinetic parameters using 1-chloro-2,4-dinitrobenzene (CDNB), GSH, p-nitrophenyl acetate (PNA) as substrates. The enzyme kinetic parameters and enzyme-substrate interaction studies demonstrated that LdGSTu1 could catalyze the conjugation of GSH to both CDNB and PNA, with a higher turnover number for CDNB than PNA. The LdGSTu1 enzyme inhibition assays demonstrated that the enzymatic conjugation of GSH to CDNB could be inhibited by multiple pesticides, suggesting a potential function of LdGSTu1 in xenobiotic adaptation.

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“…RNAi-mediated knockdown of GSTu1 in two chlorantraniliprole-resistant populations reduced the resistance of P. xylostella to chlorantraniliprole. Moreover, the activity of recombinant GSTu1 protein was inhibited by chlorantraniliprole, which suggested that the enzyme might contribute to insecticide resistance in P. xylostella [46]. The interaction between GSTu1 and chlorantraniliprole was further investigated by HPLC analysis.…”

Section: Discussionmentioning

confidence: 99%

Regulation of GSTu1-mediated insecticide resistance in Plutella xylostella by miRNA and lncRNA

Zhu

Wei

et al. 2021

PLoS Genet

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The evolution of resistance to insecticides is well known to be closely associated with the overexpression of detoxifying enzymes. Although the role of glutathione S-transferase (GST) genes in insecticide resistance has been widely reported, the underlying regulatory mechanisms are poorly understood. Here, one GST gene (GSTu1) and its antisense transcript (lnc-GSTu1-AS) were identified and cloned, and both of them were upregulated in several chlorantraniliprole-resistant Plutella xylostella populations. GSTu1 was confirmed to be involved in chlorantraniliprole resistance by direct degradation of this insecticide. Furthermore, we demonstrated that lnc-GSTu1-AS interacted with GSTu1 by forming an RNA duplex, which masked the binding site of miR-8525-5p at the GSTu1-3′UTR. In summary, we revealed that lnc-GSTu1-AS maintained the mRNA stability of GSTu1 by preventing its degradation that could have been induced by miR-8525-5p and thus increased the resistance of P. xylostella to chlorantraniliprole. Our findings reveal a new noncoding RNA-mediated pathway that regulates the expression of detoxifying enzymes in insecticide-resistant insects and offer opportunities for the further understanding of the mechanisms of insecticide and drug resistance.

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Biochemical characterization of an unclassified glutathione <i>S</i>-transferase of <i>Plutella xylostella</i>

Cited by 7 publications

References 28 publications

Structural and Functional Characterization of One Unclassified Glutathione S-Transferase in Xenobiotic Adaptation of Leptinotarsa decemlineata

Structural and Functional Characterization of One Unclassified Glutathione S-Transferase in Xenobiotic Adaptation of Leptinotarsa decemlineata

Structure and function of one unclassified-class glutathioneS-transferase inLeptinotarsa decemlineata

Regulation of GSTu1-mediated insecticide resistance in Plutella xylostella by miRNA and lncRNA

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