An Expanded Survey of the Moth PBP/GOBP Clade in Bombyx mori: New Insight into Expression and Functional Roles

Guo, Xia; Xuan, Ning; Liu, Guoxia; Xie, Hongyan; Lou, Qinian; Arnaúd, Philippe; Offmann, Bernard; Picimbon, Jean-François

doi:10.3389/fphys.2021.712593

Cited by 10 publications

(10 citation statements)

References 113 publications

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“…These results support a potential function of sex pheromone component detection by H. cunea females. Similar results were also reported in other moths, such as A. lepigone , Bombyx mori , C. sasakii , Cydia pomonella , Grapholita molesta, H. armigera , and P. xyllostella 23,51,52 . In fact, expression of HcunGOBPs2 in the antennae regardless of sexes were shown approximately five times higher than that of HcunGOBPs1 , suggesting that HcunGOBPs2 may play more vital roles in the perception of female sex pheromones than does HcunGOBPs1 .…”

Section: Discussionsupporting

confidence: 87%

“…Similar results were also reported in other moths, such as A. lepigone, Bombyx mori, C. sasakii, Cydia pomonella, Grapholita molesta, H. armigera, and P. xyllostella. 23,51,52 In fact, expression of HcunGOBPs2 in the antennae regardless of sexes were shown approximately five times higher than that of HcunGOBPs1, suggesting that HcunGOBPs2 may play more vital roles in the perception of female sex pheromones than does HcunGOBPs1. Surprisingly, there was a trace amount of expression of HcunGOBP2 and Hcun-GOBP1 in the male thoraxes, suggesting that a possible metabolic regulation occurs at GOBP levels in the male thoraxes (and/or fat bodies) or alternative functions for these proteins other than olfaction (Fig.…”

Section: Discussionmentioning

confidence: 92%

“…Similar expression of GOBPs was also detected in metabolic tissues (e.g., thoraxes, guts, and fat bodies) of B. mori. 52 These findings may require additional investigation on the GOBPs distribution, as it is commonly considered that GOBPs is only tuned for odor detection and not for other undiscovered tasks.…”

Section: Discussionmentioning

confidence: 99%

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Functional differentiation of two general‐odorant binding proteins in Hyphantria cunea (Drury) (Lepidoptera: Erebidae)

Zhang

Purba

Sun

et al. 2023

Pest Management Science

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BACKGROUND General odor‐binding proteins (GOBPs) play critical roles in insect olfactory recognition of sex pheromones and plant volatiles. Therefore, the identification of GOBPs in Hyphantria cunea (Drury) based on their characterization to pheromone components and plant volatiles is remain unknown. RESULTS In this study, two H. cunea (HcunGOBPs) genes were cloned, and their expression profiles and odorant binding characteristics were systematically analyzed. Firstly, the tissue expression study showed that both HcunGOBP1 and HcunGOBP2 were highly expressed in the antennae of both sexes, indicating their potential involvement in the perception of sex pheromones. Secondly, these two HcunGOBPs genes were expressed in Escherichia coli and ligand binding assays were used to assess the binding affinities to its sex pheromone components including two aldehydes and two epoxides, and some plant volatiles. HcunGOBP2 showed high binding affinities to two aldehyde components (Z9, Z12, Z15‐18Ald and Z9, Z12‐18Ald), and showed low binding affinities to two epoxide components (1, Z3, Z6‐9S, 10R‐epoxy‐21Hy and Z3, Z6‐9S, 10R‐epoxy‐21Hy), whereas HcunGOBP1 showed weak but significant binding to all four sex pheromone components. Furthermore, both HcunGOBPs demonstrated variable binding affinities to the plant volatiles tested. Thirdly, in silico studies of HcunGOBPs utilized homology, structure modeling, and molecular docking revealed critical hydrophobic residues might be involved in the binding of HcunGOBPs to their sex pheromone components and plant volatiles. CONCLUSION Our study suggests that these two HcunGOBPs may serve as potential targets for future studies of HcunGOBPs ligand binding, providing insight in the mechanism of olfaction in H. cunea. © 2023 Society of Chemical Industry.

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 92%

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Functional differentiation of two general‐odorant binding proteins in Hyphantria cunea (Drury) (Lepidoptera: Erebidae)

Zhang

Purba

Sun

et al. 2023

Pest Management Science

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“…After the activation of the chemosensory receptors, odorant degrading enzymes (ODEs) rapidly degrade the odorants [ 10 ]. However, other studies have demonstrated that the expression of odorant-binding proteins in other tissues such as the salivary glands, fat body, or midgut may be associated with alternative physiological functions in the insect [ 11 , 12 , 13 ]. Some OBPs , for instance, have been found to relate to innate immunity, pesticide resistance, and anti-inflammation [ 14 , 15 , 16 ].…”

Section: Introductionmentioning

confidence: 99%

Odorant-Binding Proteins and Chemosensory Proteins in Spodoptera frugiperda: From Genome-Wide Identification and Developmental Stage-Related Expression Analysis to the Perception of Host Plant Odors, Sex Pheromones, and Insecticides

Jia

Mohamed

Cattaneo

et al. 2023

IJMS

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Spodoptera frugiperda is a worldwide generalist pest with remarkable adaptations to environments and stresses, including developmental stage-related behavioral and physiological adaptations, such as diverse feeding preferences, mate seeking, and pesticide resistance. Insects’ odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) are essential for the chemical recognition during behavioral responses or other physiological processes. The genome-wide identification and the gene expression patterns of all these identified OBPs and CSPs across developmental stage-related S. frugiperda have not been reported. Here, we screened for genome-wide SfruOBPs and SfruCSPs, and analyzed the gene expression patterns of SfruOBPs and SfruCSPs repertoires across all developmental stages and sexes. We found 33 OBPs and 22 CSPs in the S. frugiperda genome. The majority of the SfruOBP genes were most highly expressed in the adult male or female stages, while more SfruCSP genes were highly expressed in the larval or egg stages, indicating their function complementation. The gene expression patterns of SfruOBPs and SfruCSPs revealed strong correlations with their respective phylogenic trees, indicating a correlation between function and evolution. In addition, we analyzed the chemical-competitive binding of a widely expressed protein, SfruOBP31, to host plant odorants, sex pheromones, and insecticides. Further ligands binding assay revealed a broad functional related binding spectrum of SfruOBP31 to host plant odorants, sex pheromones, and insecticides, suggesting its potential function in food, mate seeking, and pesticide resistance. These results provide guidance for future research on the development of behavioral regulators of S. frugiperda or other environmentally friendly pest-control strategies.

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“…OBPs are currently considered to have multiple functions, especially when OBPs are expressed in non-olfactory tissues. For instance, a new study in Bombyx mori showed that the investigated OBPs are expressed in non-olfactory tissues at different developmental stages, strongly indicating that these OBPs have multiple functions in addition to olfactory functions [ 12 ]. Through Western blot analysis and immunofluorescence localization, AaegOBP22 was found to be expressed in male sex organs in Aedes aegypti , and to have characteristics of selective binding with various ligands [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

Key Residues Affecting Binding Affinity of Sirex noctilio Fabricius Odorant-Binding Protein (SnocOBP9) to Aggregation Pheromone

Hao

Guo

et al. 2022

IJMS

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Sirex noctilio Fabricius (Hymenoptera Siricidae) is a major quarantine pest responsible for substantial economic losses in the pine industry. To achieve better pest control, (Z)-3-decen-ol was identified as the male pheromone and used as a field chemical trapping agent. However, the interactions between odorant-binding proteins (OBPs) and pheromones are poorly described. In this study, SnocOBP9 had a higher binding affinity with Z3D (Ki = 1.53 ± 0.09 μM) than other chemical ligands. Molecular dynamics simulation and binding mode analysis revealed that several nonpolar residues were the main drivers for hydrophobic interactions between SnocOBP9 and Z3D. Additionally, computational alanine scanning results indicated that five amino acids (MET54, PHE57, PHE71, PHE74, LEU116) in SnocOBP9 could potentially alter the binding affinity to Z3D. Finally, we used single-site-directed mutagenesis to substitute these five residues with alanine. These results imply that the five residues play crucial roles in the SnocOBP9-Z3D complex. Our research confirmed the function of SnocOBP9, uncovered the key residues involved in SnocOBP9-Z3D interactions, and provides an inspiration to improve the effects of pheromone agent traps.

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An Expanded Survey of the Moth PBP/GOBP Clade in Bombyx mori: New Insight into Expression and Functional Roles

Cited by 10 publications

References 113 publications

Functional differentiation of two general‐odorant binding proteins in Hyphantria cunea (Drury) (Lepidoptera: Erebidae)

Functional differentiation of two general‐odorant binding proteins in Hyphantria cunea (Drury) (Lepidoptera: Erebidae)

Odorant-Binding Proteins and Chemosensory Proteins in Spodoptera frugiperda: From Genome-Wide Identification and Developmental Stage-Related Expression Analysis to the Perception of Host Plant Odors, Sex Pheromones, and Insecticides

Key Residues Affecting Binding Affinity of Sirex noctilio Fabricius Odorant-Binding Protein (SnocOBP9) to Aggregation Pheromone

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