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 AbstractAnodic alumina coating for extraction of volatile organic compounds in human exhaled breath vapor    Next AbstractAdsorption of volatile organic compounds onto natural porous minerals »

Sci Rep


Title:"Molecular and Functional Characterization of pheromone binding protein 1 from the Oriental Fruit Moth, Grapholita molesta (Busck)"
Author(s):Zhang G; Chen J; Yu H; Tian X; Wu J;
Address:"Institute of Entomology, College of Agriculture, Yangtze University, Jingzhou, Hubei, 434025, China. ghzhang84@sina.com. Institute of Entomology, College of Agriculture, Yangtze University, Jingzhou, Hubei, 434025, China. Wuwei Academy of Forestry Science, Wuwei, Gansu, 733000, China. College of Life Science, Yangtze University, Jingzhou, Hubei, 434025, China. College of Plant Protection, North West A&F University, Yangling, Shaanxi, 712100, China"
Journal Title:Sci Rep
Year:2018
Volume:20180202
Issue:1
Page Number:2276 -
DOI: 10.1038/s41598-018-20719-0
ISSN/ISBN:2045-2322 (Electronic) 2045-2322 (Linking)
Abstract:"Pheromone binding protein (PBP) is thought primarily to bind and transport the sex pheromone in moths. The accumulated studies suggest that three PBPs were identified in moth species. In Grapholita molesta, the functions of GmolPBP2 and GmolPBP3 have been previously studied. However, the function of GmolPBP1 is still unclear. Furthermore, the Cydia pomonella sex pheromone Codlemone can act as a sex pheromone synergist of G. molesta. In C. pomonella, CpomPBP1 specifically bind the Codlemone. CpomPBP1 displays high identity with GmolPBP1 (70%), indicating that the two PBPs may share a similar 3D structure thus can bind the similar or same ligands. In this study, we explored the molecular and functional characterization of GmolPBP1. GmolPBP1, bearing the typical characteristics of Lepidopteran odorant binding proteins, was closest phylogenetically to CpomPBP1. Binding studies demonstrated that GmolPBP1 exhibited strong binding affinities with (Z)-8-dodecenyl alcohol, 1-dodecanol and Codlemone. Molecular docking showed that GmolPBP1 has different ligand recognition mechanism for the three ligands. Our results suggest that GmolPBP1 functions as recognizer of (Z)-8-dodecenyl alcohol and 1-dodecanol of the female sex pheromone blend, and may be the potential transporter of Codlemone, which contributes to the synergism of the pheromone response of G. molesta by Codlemone"
Keywords:"Animals Carrier Proteins/chemistry/genetics/*metabolism Dodecanol/*analogs & derivatives/metabolism Insect Proteins/chemistry/genetics/*metabolism Molecular Docking Simulation *Moths Phylogeny Protein Binding Protein Conformation Sequence Homology, Amino;"
Notes:"MedlineZhang, Guohui Chen, Jian Yu, Haili Tian, Xiaoli Wu, Junxiang eng Research Support, Non-U.S. Gov't England 2018/02/06 Sci Rep. 2018 Feb 2; 8(1):2276. doi: 10.1038/s41598-018-20719-0"

 
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 26-06-2024