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 Abstract"Immunolocalization of odorant-binding proteins in noctuid moths (Insecta, Lepidoptera)"    Next AbstractInfluence of pulsed electric field treatments on the volatile compounds of milk in comparison with pasteurized processing »

J Chem Ecol


Title:"Binding characterization of recombinant odorant-binding proteins from the parasitic wasp, Microplitis mediator (Hymenoptera: Braconidae)"
Author(s):Zhang S; Chen LZ; Gu SH; Cui JJ; Gao XW; Zhang YJ; Guo YY;
Address:"State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China"
Journal Title:J Chem Ecol
Year:2011
Volume:20101224
Issue:2
Page Number:189 - 194
DOI: 10.1007/s10886-010-9902-3
ISSN/ISBN:1573-1561 (Electronic) 0098-0331 (Linking)
Abstract:"Chemoreception in insects is mediated by small odorant-binding proteins (OBPs) that are believed to carry lipophilic stimuli to the olfactory receptor cells through the aqueous sensillar lymph. Binding experiments and recent structural studies of OBPs have illustrated their versatility and ability to accommodate ligands of different shapes and chemical structures. We expressed and purified seven recombinant OBPs (MmedOBP1-MmedOBP7) from the parasitic wasp, Microplitis mediator (Hymenoptera: Braconidae) in a prokaryotic expression system. With 4,4'-dianilino-1,1'-binaphthyl-5,5'-sulfonic acid (bis-ANS) as a fluorescent probe, the ligand-binding specificities of these seven MmedOBPs with 50 small organic compounds were investigated in vitro. The results revealed that all of the M. mediator OBPs can bind a wide variety of odorant molecules with different binding affinities. The best ligand for all seven MmedOBPs was beta-ionone. MmedOBP2 showed affinity for some aromatic compounds, whereas MmedOBP4 and MmedOBP6 bound several terpenoids. MmedOBP5 bound beta-ionone, but did not bind any of the other potential ligands that we tested"
Keywords:"Anilino Naphthalenesulfonates/chemistry/metabolism Animals Female Fluorescent Dyes/chemistry/metabolism *Hymenoptera Insect Proteins/*metabolism Male Plants/chemistry Protein Binding Receptors, Odorant/*metabolism Recombinant Proteins/*metabolism Substrat;"
Notes:"MedlineZhang, Shuai Chen, Li-Zhen Gu, Shao-Hua Cui, Jin-Jie Gao, Xi-Wu Zhang, Yong-Jun Guo, Yu-Yuan eng Research Support, Non-U.S. Gov't 2010/12/25 J Chem Ecol. 2011 Feb; 37(2):189-94. doi: 10.1007/s10886-010-9902-3. Epub 2010 Dec 24"

 
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 03-07-2024