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 AbstractEvaluation of zeolite for control of odorants emissions from simulated poultry manure storage    Next AbstractThe Correlation between Volatile Compounds Emitted from Sitophilus granarius (L.) and Its Electrophysiological and Behavioral Responses »

Insect Mol Biol


Title:"Expression, purification and characterization of three odorant binding proteins from the diamondback moth, Plutella xylostella"
Author(s):Cai L; Cheng X; Qin J; Xu W; You M;
Address:"State Key Laboratory of Ecological Pest Control for Fujian/Taiwan Crops, Institute of Applied Ecology, Fujian Agriculture and Forestry University, Fuzhou, China. Joint International Research Laboratory of Ecological Pest Control, Ministry of Education, Fuzhou, China. Key Laboratory of Integrated Pest Management for Fujian-Taiwan Crops, Ministry of Agriculture, Fuzhou, China. Agricultural Sciences, College of Science, Health, Engineering and Education, Murdoch University, Murdoch, WA, Australia"
Journal Title:Insect Mol Biol
Year:2020
Volume:20200819
Issue:6
Page Number:531 - 544
DOI: 10.1111/imb.12664
ISSN/ISBN:1365-2583 (Electronic) 0962-1075 (Linking)
Abstract:"Odorant binding proteins (OBPs) are critical components in insect olfactory systems where they bind, solubilize and transport odorant molecules to receptors. Here, we cloned three OBPs (PxylGOBP1, PxylGOBP2 and PxylOBP24) from the diamondback moth, Plutella xylostella, one of the most destructive pests of cruciferous crops. These three OBPs were expressed in Escherichia coli as recombinant proteins, purified and characterized by fluorescence binding assays with 39 ligands including sex pheromone and plant-derived chemical compounds. PxylGOBP1 and PxylGOBP2 showed significantly different binding affinities to theses ligands, suggesting distinct binding preferences of these two general odorant binding proteins. PxylOBP24 showed no or extremely low binding activities to selected ligands, suggesting it may be involved in non-olfactory functions. Circular dichroism spectral results demonstrated that PxylGOBP1 and PxylGOBP2 shared similar secondary structures while PxylOBP24 was significantly different. This study improves our knowledge of insect OBPs, which will assist in a better understanding of insect olfactory system and developing more environmentally friendly pest control strategies for P. xylostella"
Keywords:"Animals Female Insect Proteins/*genetics/metabolism Male Moths/*genetics/metabolism Receptors, Odorant/*genetics/metabolism OBPs binding assay insect olfaction protein purification;"
Notes:"MedlineCai, L Cheng, X Qin, J Xu, W You, M eng Research Support, Non-U.S. Gov't England 2020/07/28 Insect Mol Biol. 2020 Dec; 29(6):531-544. doi: 10.1111/imb.12664. Epub 2020 Aug 19"

 
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 06-07-2024