Journal Article

The Drosophila odorant-binding protein 28a is involved in the detection of the floral odour ß-ionone

Université Bourgogne Franche-Comté [COMUE] (UBFC), Gonzalez, Daniel, Poirier, Nicolas, The Institut National de la Recherche Agronomique, the Centre National de la Recherche Scientifique, the Université de Bourgogne-Franche Comté, the Bourgogne-Franche Comté Regional Council (PARI 2010–2011–2012, AGRALE1 Project), Institut d'écologie et des sciences de l'environnement de Paris (iEES Paris) ; Institut National de la Recherche Agronomique (INRA)-Sorbonne Université (SU)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Chertemps, Thomas, Maïbèche, Martine, Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA) ; Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Rihani, Karen, Gotthard, Guillaume, Br

2020

Overview

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.

• Publisher: Springer Verlag,CCSD,Springer International Publishing,Springer Nature B.V
• Subject: Acids / Animals / Biochemistry / Biochemistry, Molecular Biology / Biomedical and Life Sciences / Biomedicine / Cell Biology / Cellular Biology / Chemicals / Chromatography / Crystal structure / Drosophila / Drosophila melanogaster - metabolism / Drosophila melanogaster - physiology / Drosophila Proteins - chemistry / Drosophila Proteins - genetics / Drosophila Proteins - metabolism / Flowers & plants / Fluorescence / Fruit flies / Gene Deletion / Genes / Hydrophobicity / Insects / Intercellular Signaling Peptides and Proteins - chemistry / Intercellular Signaling Peptides and Proteins - genetics / Intercellular Signaling Peptides and Proteins - metabolism / Ionone / Life Sciences / Ligands / lymph / mutants / Natural environment / Norisoprenoids / Odor / odor compounds / Odorant receptors / Odorant-binding protein / Odorants / odors / Organic chemistry / Original / Original Article / Pheromones / Physiology / Protein Conformation / Proteins / Receptors / Receptors, Odorant - chemistry / Receptors, Odorant - genetics / Receptors, Odorant - metabolism / Smell / Transport / Yeast
• ISBN: 0005434497000