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" |
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" |