Chemoperception is critical for animals to detect nutritive food and avoid toxic compounds. As many other insects, Drosophila melanogaster uses various semiochemicals including pheromones and food volatiles to identify a suitable ecological niche and a mating partner. Chemosensory detection is mostly mediated by olfactory and gustatory systems involving several multigene chemoreceptor families. Volatile and non-volatile chemicals compounds entering into the sensory organ (sensillum) must be solubilized before being transported through the hydrophilic sensillum lymph bathing the chemosensory neurons. Such perireceptor events involve a family of soluble proteins named odorant-binding proteins (OBPs). Although OBPs have been the subject of numerous investigations in many insect species, their physiological function is still elusive. Supported by their relatively low affinity for odorants and their abundance in the sensilla lymph, OBPs have been hypothesized to transport hydrophobic odorant molecules to the ORs across the aqueous sensilla lymph. In addition to its solubilization role, OBPs have been proposed to play a role as a scavenger in the elimination of odorants after olfactory receptor binding. The aim of my thesis was the structural and functional characterization of some OBPs Drosophila melanogaster. Four aspects of characterization of OBP were addressed during my thesis. The structural aspect, which includes cloning, production using eukaryotic yeast Pichia pastoris, purification and crystallization of OBPs, were the first step. Then the binding properties of these OBPs were studied by identifying their potential ligands using a fluorescence binding assay. The expression pattern of these proteins was carried out and the physiological role of the OBP was identified using behavioral and electrophysiological tests on genetic mutants of Drosophila.
Rihani K, Fraichard S, Chauvel I, Poirier N, Delompré T, Neiers F, Tanimura T, Ferveur J.F and Briand L.
Communications Biology • November 22 th 2019 doi: 10.1038/s42003-019-0673-2.
Gonzalez D, Rihani K, Neiers F, Poirier N, Fraichard S, Gotthard G, Chertemps T, Maïbèche M, Ferveur J.F and Briand L.
Cellular and Molecular Life Sciences • September 28 th 2019 doi: 10.1007/s00018-019-03300-4.
Ferveur J.F, Cortot J, Rihani K, Cobb M, Everaerts C.
PeerJ • February 12th 2018 doi: 10.7717/peerj.4318.
A conserved odorant binding protein is required for amino acid detection in Drosophila melanogaster.
A conserved odorant binding protein is required for amino acid detection in Drosophila melanogaster.
The implication of OBP19b in the taste perception of amino acid in Drosophila melanogaster.
The implication of OBP19b in the taste perception of amino acid in Drosophila melanogaster.
Des drosophiles qui ne sentent pas la violette...
The implication of OBP28a in Drosophila melanogaster chemosensory perception.
Role of Odorant Binding Protein 28a in Drosophila melanogaster chemosensory perception.
Poster entitled: OBP19b is involved in the taste perception of amino acid in Drosophila melanogaster.
Poster entitled: Function of odorant-binding proteins in the Drosophila melanogaster chemoreception.
Poster entitled: Function of odorant-binding proteins in the Drosophila melanogaster chemoreception.