Download MendeleyThe Drosophila odorant-binding protein 28a is involved in the detection of the floral odour ss-ionone.
Gonzalez, D., Rihani, K., Neiers, F., Poirier, N., Fraichard, S., Gotthard, G., Chertemps, T., Maibeche, M., Ferveur, J.F., Briand, L.(2020) Cell Mol Life Sci 77: 2565-2577
- PubMed: 31564000
- DOI: https://doi.org/10.1007/s00018-019-03300-4
- Primary Citation of Related Structures:
6QQ4 - PubMed 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.
Organizational Affiliation:
AgroSup Dijon, CNRS, INRA, Université de Bourgogne-Franche Comté, Centre des Sciences du Goût et de l'Alimentation, 21000, Dijon, France.
