TAILIEUCHUNG - Báo cáo khoa học: Characterization of a chemosensory protein (ASP3c) from honeybee (Apis mellifera L.) as a brood pheromone carrier

Chemosensory proteins (CSPs) are ubiquitous soluble small proteins isolated from sensory organs of a wide range of insect species, whichare believedtobeinvolvedinchemical communication. We report the cloning of a honeybee CSP gene called ASP3c, as well as the structural and functional characterization of the encoded protein. The protein was heterologously secretedby the yeastPichia pastorisusing the native signal peptide. | Eur. J. Biochem. 269 4586-4596 2002 FEBS 2002 doi Characterization of a chemosensory protein ASP3c from honeybee Apis mellifera L. as a brood pheromone carrier Lo ic Briand1 Nicharat Swasdipan2 Claude Nespoulous1 Valerie Bezirard1 Florence Blon1 Jean-Claude Huet1 Paul Ebert2 and Jean-Claude Pernollet1 1 Biochimie et Structure des Proteines Unite de recherches INRA 477 Jouy-en-Josas Cedex France department of Biochemistry and Molecular Biology University of Queensland St Lucia Australia Chemosensory proteins CSPs are ubiquitous soluble small proteins isolated from sensory organs of a wide range of insect species which are believed to be involved in chemical communication. We report the cloning of a honeybee CSP gene called ASP3c as well as the structural and functional characterization of the encoded protein. The protein was heterologously secreted by the yeast Pichia pastoris using the native signal peptide. ASP3c disulfide bonds were assigned after trypsinolysis followed by chromatography and mass spectrometry combined with microsequencing. The pairing Cys I -Cys II Cys III -Cys IV was found to be identical to that of Schistocerca gregaria CSPs suggesting that this pattern occurs commonly throughout the insect CSPs. CD measurements revealed that ASP3c mainly consists of a-helices like other insect CSPs. Gel filtration analysis showed that ASP3c is monomeric at neutral pH. Using ASA a fluorescent fatty acid anthroyloxy analogue as a probe ASP3c was shown to bind specifically to large fatty acids and ester derivatives which are brood pheromone components in the micromolar range. It was unable to bind tested general odorants and other tested pheromones sexual and nonsexual . This is the first report on a natural pheromonal ligand bound by a recombinant CSP with a measured affinity constant. Keywords Apis mellifera L. brood pheromone chemosen-sory protein lipid-binding protein olfaction. In insect antennae the first step in chemical .

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