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Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta

Insect pheromone-binding proteins (PBPs) have been proposed to capture and transport hydrophobic sex pheromone components emitted by con-specific insects to pheromone receptors in the hemolymph of male antennal sensilla. In this study, field trapping results indicate that a mixture of E11–16: Ald an...

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Autores principales: Fang, Nainai, Hu, Yuwei, Mao, Bin, Bi, Jie, Zheng, Ya, Guan, Chuxiong, Wang, Yufeng, Li, Jihu, Mao, Yongkai, Ai, Hui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6050284/
https://www.ncbi.nlm.nih.gov/pubmed/30018452
http://dx.doi.org/10.1038/s41598-018-29164-5
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author Fang, Nainai
Hu, Yuwei
Mao, Bin
Bi, Jie
Zheng, Ya
Guan, Chuxiong
Wang, Yufeng
Li, Jihu
Mao, Yongkai
Ai, Hui
author_facet Fang, Nainai
Hu, Yuwei
Mao, Bin
Bi, Jie
Zheng, Ya
Guan, Chuxiong
Wang, Yufeng
Li, Jihu
Mao, Yongkai
Ai, Hui
author_sort Fang, Nainai
collection PubMed
description Insect pheromone-binding proteins (PBPs) have been proposed to capture and transport hydrophobic sex pheromone components emitted by con-specific insects to pheromone receptors in the hemolymph of male antennal sensilla. In this study, field trapping results indicate that a mixture of E11–16: Ald and Z11–16: Ald can effectively attract a great number of male Tryporyza intacta. Real-time PCR results suggest that the transcript levels of three TintPBP1-3 genes are mainly expressed in the adult antennae. Fluorescence competitive binding experiments show that TintPBP1-3 proteins have great binding affinities to their major sex pheromones. Moreover, TintPBPs clearly cannot bind to other four kinds of sex pheromone components released by another sugarcane borer, Chilo venosatus and Chilo infuscatellu, which have the same host plant and live in similar habitats like T. intacta. The molecular docking results demonstrate that six amino acid residues of the three TintPBPs are crucial for the specific perception of the sex pheromone components. These results will provide a foundation for the development of novel sex pheromone analogues and blocking agents for biological control of sugarcane pests, improving their efficient monitoring and integrated management strategies in the sugarcane field.
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spelling pubmed-60502842018-07-19 Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta Fang, Nainai Hu, Yuwei Mao, Bin Bi, Jie Zheng, Ya Guan, Chuxiong Wang, Yufeng Li, Jihu Mao, Yongkai Ai, Hui Sci Rep Article Insect pheromone-binding proteins (PBPs) have been proposed to capture and transport hydrophobic sex pheromone components emitted by con-specific insects to pheromone receptors in the hemolymph of male antennal sensilla. In this study, field trapping results indicate that a mixture of E11–16: Ald and Z11–16: Ald can effectively attract a great number of male Tryporyza intacta. Real-time PCR results suggest that the transcript levels of three TintPBP1-3 genes are mainly expressed in the adult antennae. Fluorescence competitive binding experiments show that TintPBP1-3 proteins have great binding affinities to their major sex pheromones. Moreover, TintPBPs clearly cannot bind to other four kinds of sex pheromone components released by another sugarcane borer, Chilo venosatus and Chilo infuscatellu, which have the same host plant and live in similar habitats like T. intacta. The molecular docking results demonstrate that six amino acid residues of the three TintPBPs are crucial for the specific perception of the sex pheromone components. These results will provide a foundation for the development of novel sex pheromone analogues and blocking agents for biological control of sugarcane pests, improving their efficient monitoring and integrated management strategies in the sugarcane field. Nature Publishing Group UK 2018-07-17 /pmc/articles/PMC6050284/ /pubmed/30018452 http://dx.doi.org/10.1038/s41598-018-29164-5 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Fang, Nainai
Hu, Yuwei
Mao, Bin
Bi, Jie
Zheng, Ya
Guan, Chuxiong
Wang, Yufeng
Li, Jihu
Mao, Yongkai
Ai, Hui
Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta
title Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta
title_full Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta
title_fullStr Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta
title_full_unstemmed Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta
title_short Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta
title_sort molecular characterization and functional differentiation of three pheromone-binding proteins from tryporyza intacta
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6050284/
https://www.ncbi.nlm.nih.gov/pubmed/30018452
http://dx.doi.org/10.1038/s41598-018-29164-5
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