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 AbstractDetermination of hazardous volatile organic compounds in the Hoffmann list by ion-molecule reaction mass spectrometry    Next AbstractAdsorption of Fluorocarbons and Chlorocarbons by Highly Porous and Robust Fluorinated Zirconium Metal-Organic Frameworks »

Environ Entomol


Title:"Molecular Identification, Expression, and Functional Analysis of a General Odorant-Binding Protein 1 of Asian Citrus Psyllid"
Author(s):Wang H; Chen H; Wang Z; Liu J; Zhang X; Li C; Zeng X;
Address:"Guangdong Engineering Research Center for Insect Behavior Regulation, College of Agriculture South China Agricultural University, Guangzhou, China. Guangdong Key Laboratory of Animal Conservation and Resource Utilization, Guangdong Public Laboratory of Wild Animal Conservation and Utilization, Guangdong Institute of Applied Biological Resources, Guangzhou, Guangdong, China"
Journal Title:Environ Entomol
Year:2019
Volume:48
Issue:1
Page Number:245 - 252
DOI: 10.1093/ee/nvy179
ISSN/ISBN:1938-2936 (Electronic) 0046-225X (Linking)
Abstract:"For insects, odorant-binding proteins (OBPs) play an essential role in binding and transporting semiochemicals through the sensillum lymph to olfactory receptor neurons within the antennal sensilla. In the present study, the full-length cDNA encoding a general odorant-binding protein 1 (DcitOBP1, accession number KY475564) was cloned from the antennae of Diaphorina citri using RACE-PCR, and qRT-PCR analysis revealed that the DcitOBP1 gene was expressed mainly in the antennae of D. citri. In molecular docking assay, the results showed that DcitOBP1 protein has better binding affinities to the 12 selected host-plant volatile compounds. Then, the recombinant DcitOBP1 protein was expressed in Escherichia coli. After removed His-Tag, the binding properties of purified DcitOBP1 protein to the selected host-plant volatile compounds were investigated in a fluorescence ligand-binding assay, similar, but more obviously binding properties of DcitOBP1 protein result were obtained, the dissociation constant (KD) value of DcitOBP1/1-NPN complex was 6.440 +/- 0.521, and the DcitOBP1 protein showed high binding affinities (IC50 < 100 muM) to six of the selected ligands, namely methyl salicylate, alpha-phellandrene, (1R)-(+)-alpha-pinene, 3-carene, beta-caryophyllene, and alpha-caryophyllene. Additionally, the behavior bioassays were also showed that D. citri had significant behavioral responses toward to alpha-caryophyllene, beta-caryophyllene, (1R)-(+)-alpha-pinene, and alpha-phellandrene. Our investigation infer that the DcitOBP1 protein might play a crucial role in host-plant volatile odorants' perception in D. citri, and these results also have been supplied previous insight evidence into the physiological functions of the DcitOBP1 protein of D. citri"
Keywords:"Amino Acid Sequence Animals Arthropod Antennae/*metabolism Base Sequence Behavior, Animal Female Hemiptera/genetics/*metabolism Male Molecular Docking Simulation Receptors, Odorant/genetics/*metabolism Sequence Analysis, DNA Volatile Organic Compounds;"
Notes:"MedlineWang, Huatang Chen, Huiling Wang, Zhengbing Liu, Jiali Zhang, Xingyan Li, Chaofeng Zeng, Xinnian eng Research Support, Non-U.S. Gov't England 2018/12/20 Environ Entomol. 2019 Feb 13; 48(1):245-252. doi: 10.1093/ee/nvy179"

 
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 26-12-2024