A sublethal dose of neonicotinoid imidacloprid precisely sensed and detoxified by a C-minus odorant-binding protein 17 highly expressed in the legs of Apis cerana

Qiu, Yi-Lei; Wu, Fan; Zhang, Li; Jiang, Hu-Qiang; Chen, Jintao; Pan, Ying-Jia; Li, Hongliang

doi:10.1016/j.scitotenv.2023.163762

Cited by 4 publications

(2 citation statements)

References 45 publications

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“…Other than acute effects on target insect pests, chemical insecticides cause serious negative effects on nontarget insects, such as parasitoid wasps and pollinators ( 162 ). Several studies reported that the OBP either showed high binding affinity to insecticides ( 154 , 158 ) or the binding of OBP to floral volatile was significantly affected by insecticides ( 163 ). These studies implied that OBPs may contribute to olfaction based behavioral response to insecticides.…”

Section: Diverse Roles Of Insect Obps In Communication and Xenobiotic...mentioning

confidence: 99%

Roles of insect odorant binding proteins in communication and xenobiotic adaptation

Abendroth,

Moural,

Wei

et al. 2023

Front. Insect Sci.

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Odorant binding proteins (OBPs) are small water-soluble proteins mainly associated with olfaction, facilitating the transport of odorant molecules to their relevant receptors in the sensillum lymph. While traditionally considered essential for olfaction, recent research has revealed that OBPs are engaged in a diverse range of physiological functions in modulating chemical communication and defense. Over the past 10 years, emerging evidence suggests that OBPs play vital roles in purifying the perireceptor space from unwanted xenobiotics including plant volatiles and pesticides, potentially facilitating xenobiotic adaptation, such as host location, adaptation, and pesticide resistance. This multifunctionality can be attributed, in part, to their structural variability and effectiveness in transporting, sequestering, and concealing numerous hydrophobic molecules. Here, we firstly overviewed the classification and structural properties of OBPs in diverse insect orders. Subsequently, we discussed the myriad of functional roles of insect OBPs in communication and their adaptation to xenobiotics. By synthesizing the current knowledge in this field, our review paper contributes to a comprehensive understanding of the significance of insect OBPs in chemical ecology, xenobiotic adaptation, paving the way for future research in this fascinating area of study.

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Section: Diverse Roles Of Insect Obps In Communication and Xenobiotic...mentioning

confidence: 99%

Roles of insect odorant binding proteins in communication and xenobiotic adaptation

Abendroth,

Moural,

Wei

et al. 2023

Front. Insect Sci.

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“…Subsequently, qRT-PCR was employed to investigate their relative expression across different developmental stages and tissues. The recombinant proteins were purified using an Escherichia coli expression system for these three CpomGOBP2 proteins [26,27]. Finally, the recombinant proteins were utilized to estimate their binding affinities to host plant volatiles and sex pheromone components using competitive fluorescence binding assays.…”

Section: Introductionmentioning

confidence: 99%

Molecular and Functional Characterization of Three General Odorant-Binding Protein 2 Genes in Cydia pomonella (Lepidoptera: Tortricidae)

Zhou,

Huang,

et al. 2024

IJMS

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General odorant-binding proteins (GOBPs) play a crucial role in the detection of host plant volatiles and pheromones by lepidopterans. Previous studies identified two duplications in the GOBP2 gene in Cydia pomonella. In this study, we employed qRT-PCR, protein purification, and fluorescence competitive binding assays to investigate the functions of three GOBP2 genes in C. pomonella. Our findings reveal that CpomGOBP2a and CpomGOBP2b are specifically highly expressed in antennae, while CpomGOBP2c exhibits high specific expression in wings, suggesting a potential divergence in their functions. Recombinant proteins of CpomGOBP2a, CpomGOBP2b, and CpomGOBP2c were successfully expressed and purified, enabling an in-depth exploration of their functions. Competitive binding assays with 20 host plant volatiles and the sex pheromone (codlemone) demonstrated that CpomGOBP2a exhibits strong binding to four compounds, namely butyl octanoate, ethyl (2E,4Z)-deca-2,4-dienoate (pear ester), codlemone, and geranylacetone, with corresponding dissolution constants (Ki) of 8.59993 μM, 9.14704 μM, 22.66298 μM, and 22.86923 μM, respectively. CpomGOBP2b showed specific binding to pear ester (Ki = 17.37481 μM), while CpomGOBP2c did not exhibit binding to any tested compounds. In conclusion, our results indicate a functional divergence among CpomGOBP2a, CpomGOBP2b, and CpomGOBP2c. These findings contribute valuable insights for the development of novel prevention and control technologies and enhance our understanding of the evolutionary mechanisms of olfactory genes in C. pomonella.

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New and emerging mechanisms of insecticide resistance

Pu,

Chung

2024

Current Opinion in Insect Science

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A sublethal dose of neonicotinoid imidacloprid precisely sensed and detoxified by a C-minus odorant-binding protein 17 highly expressed in the legs of Apis cerana

Cited by 4 publications

References 45 publications

Roles of insect odorant binding proteins in communication and xenobiotic adaptation

Roles of insect odorant binding proteins in communication and xenobiotic adaptation

Molecular and Functional Characterization of Three General Odorant-Binding Protein 2 Genes in Cydia pomonella (Lepidoptera: Tortricidae)

New and emerging mechanisms of insecticide resistance

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