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Proteomic analysis and ligand-binding studies of the odorant-binding protein OBP1 in the elephant's trunk

ABSTRACT: Chemical communication in elephants has been studied in detail both at the chemical and at the behavioural levels. Several pheromones have been identified, and their specific effects on the sexual behaviour of both the African and the Asian elephants have been accurately documented. This work is focused on the characterization of OBP1 through ligand-binding studies and analysis of post-translational modifications (PTMs). First, we have performed a proteomic analysis of a crude extract of the trunk wash obtained from the African elephant, and have found OBP1 as the main component, together with minor amounts of a OBP1 isoform and the von Ebner's gland (VEG) protein. Proteomic analysis of OBP1 revealed the occurrence of a variable degree of O-glycosylation, phosphorylation and acetylation in this protein. To specifically assay OBP1 spectra of binding, we have then expressed the African elephant protein in Pichia pastoris, which showed PTMs very similar to the natural counterpart. At functional level, we have found that recombinant OBP1 from the African elephant is able to bind the sex pheromone (Z)-7-dodecenyl acetate with strong affinity and some structurally related esters with lower strength.

INSTRUMENT(S):

ORGANISM(S): Loxodonta Africana (african Elephant)

SUBMITTER: CHIARA D'AMBROSIO