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Odorant and pheromone binding by aphrodisin, a hamster aphrodisiac protein
Author(s) -
Briand Loı̈c,
Huet Jean-Claude,
Perez Valérie,
Lenoir Guillaume,
Nespoulous Claude,
Boucher Yves,
Trotier Didier,
Pernollet Jean-Claude
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01719-1
Subject(s) - pichia pastoris , pheromone , biochemistry , aphrodisiac , recombinant dna , chemistry , glycoprotein , hamster , yeast , receptor , biology , microbiology and biotechnology , botany , medicine , alternative medicine , pathology , gene
Aphrodisin is a soluble glycoprotein of hamster vaginal discharges, which stimulates male copulatory behavior. Natural aphrodisin was purified and its post‐translational modifications characterized by MALDI‐MS peptide mapping. To evaluate its ability to bind small volatile ligands, the aphrodisiac protein was expressed in the yeast Pichia pastoris as two major isoforms differing in their glycosylation degree, but close in conformation to the natural protein. Dimeric recombinant aphrodisins were equally able to efficiently bind odors (2‐isobutyl‐3‐methoxypyrazine and methyl thiobutyrate) and a pheromone (dimethyl disulfide), suggesting that they could act as pheromone carriers instead of, or in addition to, direct vomeronasal neuron receptor activators.