Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractIdentification of Key Residues in the NisK Sensor Region for Nisin Biosynthesis Regulation    Next AbstractAssessment of fresh Alpinia galanga (A. galanga) drying techniques for the chemical composition of essential oil and its antioxidant and biological activity »

Front Physiol


Title:Binding Specificity of Two PBPs in the Yellow Peach Moth Conogethes punctiferalis (Guenee)
Author(s):Ge X; Ahmed T; Zhang T; Wang Z; He K; Bai S;
Address:"State Key Laboratory for Biology of Plant Disease and Insect Pest, Institute of Plant Protection, Chinese Academy of Agricultural Science, Beijing, China. Department of Plant Protection, Henan Institute of Science and Technology, Xinxiang, China. Bangladesh Sugarcrop Research Institute, Pabna, Bangladesh"
Journal Title:Front Physiol
Year:2018
Volume:20180403
Issue:
Page Number:308 -
DOI: 10.3389/fphys.2018.00308
ISSN/ISBN:1664-042X (Print) 1664-042X (Electronic) 1664-042X (Linking)
Abstract:"Pheromone binding proteins (PBPs) play an important role in olfaction of insects by transporting sex pheromones across the sensillum lymph to odorant receptors. To obtain a better understanding of the molecular basis between PBPs and semiochemicals, we have cloned, expressed, and purified two PBPs (CpunPBP2 and CpunPBP5) from the antennae of Conogethes punctiferalis. Fluorescence competitive binding assays were used to investigate binding affinities of CpunPBP2 and CpunPBP5 to sex pheromone and volatiles. Results indicate both CpunPBP2 and CpunPBP5 bind sex pheromones E10-16:Ald, Z10-16:Ald and hexadecanal with higher affinities. In addition, CpunPBP2 and CpunPBP5 also could bind some odorants, such as 1-tetradecanol, trans-caryopyllene, farnesene, and beta-farnesene. Homology modeling to predict 3D structure and molecular docking to predict key binding sites were used, to better understand interactions of CpunPBP2 and CpunPBP5 with sex pheromones E10-16:Ald and Z10-16:Ald. According to the results, Phe9, Phe33, Ser53, and Phe115 were key binding sites predicted for CpunPBP2, as were Ser9, Phe12, Val115, and Arg120 for CpunPBP5. Binding affinities of four mutants of CpunPBP2 and four mutants of CpunPBP5 with the two sex pheromones were investigated by fluorescence competitive binding assays. Results indicate that single nucleotides mutation may affect interactions between PBPs and sex pheromones. Expression levels of CpunPBP2 and CpunPBP5 in different tissues were evaluated using qPCR. Results show that CpunPBP2 and CpunPBP5 were largely amplified in the antennae, with low expression levels in other tissues. CpunPBP2 was expressed mainly in male antennae, whereas CpunPBP5 was expressed mainly in female antennae. These results provide new insights into understanding the recognition between PBPs and ligands"
Keywords:Conogethes punctiferalis fluorescence competitive binding assays molecular docking pheromone binding proteins qPCR;
Notes:"PubMed-not-MEDLINEGe, Xing Ahmed, Tofael Zhang, Tiantao Wang, Zhenying He, Kanglai Bai, Shuxiong eng Switzerland 2018/04/19 Front Physiol. 2018 Apr 3; 9:308. doi: 10.3389/fphys.2018.00308. eCollection 2018"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 20-11-2024