Odorant and pheromone binding by aphrodisin, a hamster aphrodisiac protein

FEBS Letters

Lenoir, Guillaume¹  Trotier, Didier²  Perez, Valérie¹  Pernollet, Jean-Claude¹  Briand, Loı̈c¹  Boucher, Yves²  Huet, Jean-Claude¹  Nespoulous, Claude¹ 

[1] Biochimie et Structure des Protéines, INRA UR 477, Domaine de Vilvert, F-78352 Jouy-en-Josas Cedex, France;Neurobiologie Sensorielle, E.P.H.E., 1 Avenue des Olympiades, F-91305 Massy, France

关键词: Aphrodisin;    Glycosylation;    Hamster;    Recombinant protein expression;    Vaginal discharge protein;    Vomeronasal organ;    Aphro-Nat;    natural aphrodisin;    Aphro-RecG;    recombinant glycosylated aphrodisin;    Aphro-RecNG;    recombinant unglycosylated aphrodisin;    DMDS;    dimethyl disulfide;    GlcNAc;    N-acetylglucosamine;    IBMP;    2-isobutyl-3-methoxypyrazine;    ES-MS;    electrospray mass spectrometry;    LC–MS;    liquid chromatography coupled with mass spectrometry;    MALDI-MS;    time of flight matrix-assisted laser desorption ionization mass spectrometry;    MTB;    methyl thiobutyrate;    OBP;    odorant binding protein;    RPLC;    reversed-phase HPLC;   

DOI  :  10.1016/S0014-5793(00)01719-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown