Odorant and pheromone binding by aphrodisin, a hamster aphrodisiac protein

被引：49

作者：

Briand, L

Huet, JC

Perez, V

Lenoir, C

Nespoulous, C

Boucher, Y

Trotier, D

Pernollet, JC

机构：

[1] INRA UR 477, F-78352 Jouy En Josas, France

[2] EPHE, F-91305 Massy, France

[3] Univ Paris 07, F-75251 Paris, France

来源：

FEBS LETTERS | 2000年 / 476卷 / 03期

关键词：

aphrodisin; glycosylation; hamster; recombinant protein expression; vaginal discharge protein; vomeronasal organ;

D O I：

10.1016/S0014-5793(00)01719-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：179 / 185

页数：7

共 44 条

[1]

ANHOLT RRH, 1986, J NEUROSCI, V6, P1962

[2] FORMATION OF THE EXTRACELLULAR MUCOUS MATRIX OF OLFACTORY NEUROEPITHELIUM - IDENTIFICATION OF PARTIALLY GLYCOSYLATED AND NONGLYCOSYLATED PRECURSORS OF OLFACTOMEDIN [J].