Odorant-binding protein 76a (LUSH) (LUSH)

LUSH (Odorant-binding protein 76a) is a specialized extracellular protein found in the olfactory sensilla of the fruit fly, Drosophila melanogaster [1]. It belongs to the odorant-binding protein (OBP) family, which is characterized by a small, globular structure stabilized by three conserved disulfide bonds [1]. LUSH is primarily known for its essential role in the detection of the male-specific pheromone 11-cis-vaccenyl acetate (cVA), which is crucial for regulating social and mating behaviors [2]. Beyond pheromone transport, LUSH is involved in the fly's chemosensory response to alcohols, such as ethanol and propanol, which influenced its naming [4]. Mechanistically, LUSH acts as a carrier for hydrophobic ligands through the aqueous sensillum lymph, but it also undergoes a specific conformational change upon binding cVA that is required to activate the Or67d/Orco receptor complex [3]. While LUSH is not a human therapeutic target, it serves as a fundamental model for understanding the molecular basis of olfaction and signal transduction in insects [1]. Its unique mechanism of ligand-induced conformational activation makes it a subject of interest for developing highly specific insect repellents or attractants [3]. Consequently, LUSH and its homologs are significant targets in agricultural biotechnology and public health for controlling insect populations and the spread of vector-borne diseases [2].

Other names

OBP76aOdorant-binding protein 76aLush proteinDrosophila OBP76a

LUSH functions by binding hydrophobic odorants and pheromones in the sensillum lymph and transporting them to olfactory receptors. Specifically, the binding of 11-cis-vaccenyl acetate (cVA) induces a conformational change in LUSH that directly triggers the activation of the Or67d/Orco receptor complex on sensory neurons [3].