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"Filling in sewage sludge biodrying gaps: Greenhouse gases, volatile organic compounds and odour emissions"    Next Abstract"Multipoint characterization of the emission of odour, volatile organic compounds and greenhouse gases from a full-scale membrane-based municipal WWTP" »

Cell Mol Life Sci


Title:The Drosophila odorant-binding protein 28a is involved in the detection of the floral odour ss-ionone
Author(s):Gonzalez D; Rihani K; Neiers F; Poirier N; Fraichard S; Gotthard G; Chertemps T; Maibeche M; Ferveur JF; Briand L;
Address:"AgroSup Dijon, CNRS, INRA, Universite de Bourgogne-Franche Comte, Centre des Sciences du Gout et de l'Alimentation, 21000, Dijon, France. European Synchrotron Radiation Facility, 38043, Grenoble, France. Sorbonne Universite, INRA, CNRS, IRD, UPEC, Institut d'Ecologie et des Sciences de l'Environnement de Paris, 75005, Paris, France. AgroSup Dijon, CNRS, INRA, Universite de Bourgogne-Franche Comte, Centre des Sciences du Gout et de l'Alimentation, 21000, Dijon, France. loic.briand@inra.fr"
Journal Title:Cell Mol Life Sci
Year:2020
Volume:20190928
Issue:13
Page Number:2565 - 2577
DOI: 10.1007/s00018-019-03300-4
ISSN/ISBN:1420-9071 (Electronic) 1420-682X (Linking)
Abstract:"Odorant-binding proteins (OBPs) are small soluble proteins that are thought to transport hydrophobic odorants across the aqueous sensillar lymph to olfactory receptors. A recent study revealed that OBP28a, one of the most abundant Drosophila OBPs, is not required for odorant transport, but acts in buffering rapid odour variation in the odorant environment. To further unravel and decipher its functional role, we expressed recombinant OBP28a and characterized its binding specificity. Using a fluorescent binding assay, we found that OBP28a binds a restricted number of floral-like chemicals, including ss-ionone, with an affinity in the micromolar range. We solved the X-ray crystal structure of OBP28a, which showed extensive conformation changes upon ligand binding. Mutant flies genetically deleted for the OBP28a gene showed altered responses to ss-ionone at a given concentration range, supporting its essential role in the detection of specific compounds present in the natural environment of the fly"
Keywords:"Animals Drosophila Proteins/*chemistry/genetics/*metabolism Drosophila melanogaster/metabolism/physiology Gene Deletion Intercellular Signaling Peptides and Proteins/*chemistry/genetics/*metabolism Ligands *Norisoprenoids Protein Conformation Receptors, O;"
Notes:"MedlineGonzalez, Daniel Rihani, Karen Neiers, Fabrice Poirier, Nicolas Fraichard, Stephane Gotthard, Guillaume Chertemps, Thomas Maibeche, Martine Ferveur, Jean-Francois Briand, Loic eng Switzerland 2019/09/30 Cell Mol Life Sci. 2020 Jul; 77(13):2565-2577. doi: 10.1007/s00018-019-03300-4. Epub 2019 Sep 28"

 
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 14-11-2024