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Antennal transcriptome analysis of odorant-binding proteins and characterization of GOBP2 in the variegated cutworm Peridroma saucia

Odorant-binding proteins (OBPs) are expressed at extremely high concentrations in the chemo-sensilla lymph of insects and have long been thought to be crucial for delivering the semiochemicals to the odorant receptors. They are represented by multiple classes: general odorant-binding proteins (GOBP1...

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Autores principales: Dong, Jun-Feng, Wang, Ke, Sun, Ya-Lan, Tian, Cai-Hong, Wang, Shao-Li
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10450149/
https://www.ncbi.nlm.nih.gov/pubmed/37637146
http://dx.doi.org/10.3389/fphys.2023.1241324
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author Dong, Jun-Feng
Wang, Ke
Sun, Ya-Lan
Tian, Cai-Hong
Wang, Shao-Li
author_facet Dong, Jun-Feng
Wang, Ke
Sun, Ya-Lan
Tian, Cai-Hong
Wang, Shao-Li
author_sort Dong, Jun-Feng
collection PubMed
description Odorant-binding proteins (OBPs) are expressed at extremely high concentrations in the chemo-sensilla lymph of insects and have long been thought to be crucial for delivering the semiochemicals to the odorant receptors. They are represented by multiple classes: general odorant-binding proteins (GOBP1 and GOBP2) and pheromone-binding proteins. In the current study, we identified a total of 35 OBPs in the antennal transcriptome of Peridroma saucia, a worldwide pest that causes serious damage to various crops. A gene expression value (TPM, transcripts per million) analysis revealed that seven OBPs (PsauPBP1/2/3, PsauGOBP1/2, PsauOBP6, and PsauOBP8) were highly abundant in the antennae. Next, we focused on the expression and functional characterization of PsauGOBP2. Real-time quantitative-PCR analysis demonstrated that PsauGOBP2 was predominantly expressed in the antennae of both sexes. Fluorescence binding assays showed that the recombinant PsauGOBP2 strongly binds to the female sex pheromone components Z11-16: Ac (K(i) = 4.2 μM) and Z9-14: Ac (K(i) = 4.9 μM) and binds moderately (6 µM ≤ K(i) ≤ 13 µM) to the host plant volatiles phenylethyl acetate, β-myrcene, and dodecanol. Further 3D structural modeling and molecular docking revealed that several crucial amino acid residues are involved in ligand binding. The results not only increase our understanding of the olfactory system of P. saucia but also provide insights into the function of PsauGOBP2 that has implications for developing sustainable approaches for P. saucia management.
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spelling pubmed-104501492023-08-26 Antennal transcriptome analysis of odorant-binding proteins and characterization of GOBP2 in the variegated cutworm Peridroma saucia Dong, Jun-Feng Wang, Ke Sun, Ya-Lan Tian, Cai-Hong Wang, Shao-Li Front Physiol Physiology Odorant-binding proteins (OBPs) are expressed at extremely high concentrations in the chemo-sensilla lymph of insects and have long been thought to be crucial for delivering the semiochemicals to the odorant receptors. They are represented by multiple classes: general odorant-binding proteins (GOBP1 and GOBP2) and pheromone-binding proteins. In the current study, we identified a total of 35 OBPs in the antennal transcriptome of Peridroma saucia, a worldwide pest that causes serious damage to various crops. A gene expression value (TPM, transcripts per million) analysis revealed that seven OBPs (PsauPBP1/2/3, PsauGOBP1/2, PsauOBP6, and PsauOBP8) were highly abundant in the antennae. Next, we focused on the expression and functional characterization of PsauGOBP2. Real-time quantitative-PCR analysis demonstrated that PsauGOBP2 was predominantly expressed in the antennae of both sexes. Fluorescence binding assays showed that the recombinant PsauGOBP2 strongly binds to the female sex pheromone components Z11-16: Ac (K(i) = 4.2 μM) and Z9-14: Ac (K(i) = 4.9 μM) and binds moderately (6 µM ≤ K(i) ≤ 13 µM) to the host plant volatiles phenylethyl acetate, β-myrcene, and dodecanol. Further 3D structural modeling and molecular docking revealed that several crucial amino acid residues are involved in ligand binding. The results not only increase our understanding of the olfactory system of P. saucia but also provide insights into the function of PsauGOBP2 that has implications for developing sustainable approaches for P. saucia management. Frontiers Media S.A. 2023-08-10 /pmc/articles/PMC10450149/ /pubmed/37637146 http://dx.doi.org/10.3389/fphys.2023.1241324 Text en Copyright © 2023 Dong, Wang, Sun, Tian and Wang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Dong, Jun-Feng
Wang, Ke
Sun, Ya-Lan
Tian, Cai-Hong
Wang, Shao-Li
Antennal transcriptome analysis of odorant-binding proteins and characterization of GOBP2 in the variegated cutworm Peridroma saucia
title Antennal transcriptome analysis of odorant-binding proteins and characterization of GOBP2 in the variegated cutworm Peridroma saucia
title_full Antennal transcriptome analysis of odorant-binding proteins and characterization of GOBP2 in the variegated cutworm Peridroma saucia
title_fullStr Antennal transcriptome analysis of odorant-binding proteins and characterization of GOBP2 in the variegated cutworm Peridroma saucia
title_full_unstemmed Antennal transcriptome analysis of odorant-binding proteins and characterization of GOBP2 in the variegated cutworm Peridroma saucia
title_short Antennal transcriptome analysis of odorant-binding proteins and characterization of GOBP2 in the variegated cutworm Peridroma saucia
title_sort antennal transcriptome analysis of odorant-binding proteins and characterization of gobp2 in the variegated cutworm peridroma saucia
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10450149/
https://www.ncbi.nlm.nih.gov/pubmed/37637146
http://dx.doi.org/10.3389/fphys.2023.1241324
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