Architecture and potential roles of a delta-class glutathione S-transferase in protecting honey bee from agrochemicals

The European honey bee, Apis mellifera, serves as the principle managed pollinator species globally. In recent decades, honey bee populations have been facing serious health threats from combined biotic and abiotic stressors, including diseases, limited nutrition, and agrochemical exposure. Understanding the molecular mechanisms underlying xenobiotic adaptation of A. mellifera is critical, considering its extensive exposure to phytochemicals and agrochemicals present in the environment. In this study, we conducted a comprehensive structural and functional characterization of AmGSTD1, a delta class glutathione S-transferase (GST), to unravel its roles in agrochemical detoxification and antioxidative stress responses. We determined the 3-dimensional (3D) structure of a honey bee GST using protein crystallography for the first time, providing new insights into its molecular structure. Our investigations revealed that AmGSTD1 metabolizes model substrates, including 1-chloro-2,4-dinitrobenzene (CDNB), p-nitrophenyl acetate (PNA), phenylethyl isothiocyanate (PEITC), propyl isothiocyanate (PITC), and the oxidation byproduct 4-hydroxynonenal (HNE). Moreover, we discovered that AmGSTD1 exhibits binding affinity with the fluorophore 8-Anilinonaphthalene-1-sulfonic acid (ANS), which can be inhibited with various herbicides, fungicides, insecticides, and their metabolites. These findings highlight the potential contribution of AmGSTD1 in safeguarding honey bee health against various agrochemicals, while also mitigating oxidative stress resulting from exposure to these substances.

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Work Title Architecture and potential roles of a delta-class glutathione S-transferase in protecting honey bee from agrochemicals
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Open Access
Creators
  1. Timothy W. Moural
  2. Sonu Koirala B K
  3. Gaurab Bhattarai
  4. Ziming He
  5. Haoyang Guo
  6. Ngoc T. Phan
  7. Edwin G. Rajotte
  8. David J. Biddinger
  9. Kelli Hoover
  10. Fang Zhu
Keyword
  1. Environmental stresses
License In Copyright (Rights Reserved)
Work Type Article
Publisher
  1. Chemosphere
Publication Date January 4, 2024
Publisher Identifier (DOI)
  1. https://doi.org/10.1016/j.chemosphere.2023.141089
Deposited February 12, 2024

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  • Created

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Moural_et_al._2023.pdf

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator Timothy W. Moural

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator Sonu Koirala B K

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator Gaurab Bhattarai

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator Ziming He

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator Haoyang Guo

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator Ngoc T. Phan

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator Edwin G. Rajotte

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator David J. Biddinger

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator Kelli Hoover

    February 12, 2024 06:03 by Researcher Metadata Database

  • Added Creator Fang Zhu

    February 12, 2024 06:03 by Researcher Metadata Database

  • Published

    February 12, 2024 06:03 by Researcher Metadata Database

  • Updated Keyword, Description, Publication Date Show Changes

    February 12, 2024 14:25 by avs5190

    Keyword
    • Environmental stresses
    Description
    • <p>The European honey bee, Apis mellifera, serves as the principle managed pollinator species globally. In recent decades, honey bee populations have been facing serious health threats from combined biotic and abiotic stressors, including diseases, limited nutrition, and agrochemical exposure. Understanding the molecular mechanisms underlying xenobiotic adaptation of A. mellifera is critical, considering its extensive exposure to phytochemicals and agrochemicals present in the environment. In this study, we conducted a comprehensive structural and functional characterization of AmGSTD1, a delta class glutathione S-transferase (GST), to unravel its roles in agrochemical detoxification and antioxidative stress responses. We determined the 3-dimensional (3D) structure of a honey bee GST using protein crystallography for the first time, providing new insights into its molecular structure. Our investigations revealed that AmGSTD1 metabolizes model substrates, including 1-chloro-2,4-dinitrobenzene (CDNB), p-nitrophenyl acetate (PNA), phenylethyl isothiocyanate (PEITC), propyl isothiocyanate (PITC), and the oxidation byproduct 4-hydroxynonenal (HNE). Moreover, we discovered that AmGSTD1 exhibits binding affinity with the fluorophore 8-Anilinonaphthalene-1-sulfonic acid (ANS), which can be inhibited with various herbicides, fungicides, insecticides, and their metabolites. These findings highlight the potential contribution of AmGSTD1 in safeguarding honey bee health against various agrochemicals, while also mitigating oxidative stress resulting from exposure to these substances.</p>
    • <p>The European honey bee, _Apis mellifera_, serves as the principle managed pollinator species globally. In recent decades, honey bee populations have been facing serious health threats from combined biotic and abiotic stressors, including diseases, limited nutrition, and agrochemical exposure. Understanding the molecular mechanisms underlying xenobiotic adaptation of _A. mellifera_ is critical, considering its extensive exposure to phytochemicals and agrochemicals present in the environment. In this study, we conducted a comprehensive structural and functional characterization of AmGSTD1, a delta class glutathione S-transferase (GST), to unravel its roles in agrochemical detoxification and antioxidative stress responses. We determined the 3-dimensional (3D) structure of a honey bee GST using protein crystallography for the first time, providing new insights into its molecular structure. Our investigations revealed that AmGSTD1 metabolizes model substrates, including 1-chloro-2,4-dinitrobenzene (CDNB), p-nitrophenyl acetate (PNA), phenylethyl isothiocyanate (PEITC), propyl isothiocyanate (PITC), and the oxidation byproduct 4-hydroxynonenal (HNE). Moreover, we discovered that AmGSTD1 exhibits binding affinity with the fluorophore 8-Anilinonaphthalene-1-sulfonic acid (ANS), which can be inhibited with various herbicides, fungicides, insecticides, and their metabolites. These findings highlight the potential contribution of AmGSTD1 in safeguarding honey bee health against various agrochemicals, while also mitigating oxidative stress resulting from exposure to these substances.</p>
    Publication Date
    • 2024-02-01
    • 2024-01-04
  • Updated

    April 04, 2024 10:22 by [unknown user]