Cloning and expression of a queen pheromone-binding protein in the honeybee: an olfactory-specific, developmentally regulated protein
| Autor: | Christian Ouali, Gérard Arnold, Jean-Claude Pernollet, Jean-Claude Huet, Claudine Masson, Christine Michard-Vanhée, Emmanuelle Danty, Odile Gaudemer, D. Huet, Loïc Briand, Valérie Perez |
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| Přispěvatelé: | Centre Européen des Sciences du Goût, Centre National de la Recherche Scientifique (CNRS), Unité de Recherches de Biochimie et Structure des Protéines (INRA UR 477), Institut National de la Recherche Agronomique (INRA), Neurobiologie Expérimentale et Théorie des Systèmes Complexes (CNRS UPR 9081), This work was supported by the French Centre National de la Recherche Scientifique, the Association pour la Recherche contre le Cancer, and the Institut National de la Recherche Agronomique., Centre Européen des Sciences du Goût (CESG), Université de Bourgogne (UB), Centre des Sciences du Goût (CSG), Etablissement National d'Enseignement Supérieur Agronomique de Dijon (ENESAD)-Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS), Unité de recherche Biochimie et Structure des Protéines (UBSP), BERGER, Emmanuelle |
| Jazyk: | angličtina |
| Rok vydání: | 1999 |
| Předmět: |
0106 biological sciences
Male MESH: Sequence Homology Amino Acid clonage moléculaire [SDV]Life Sciences [q-bio] régulation physiologique MESH: Amino Acid Sequence antenne MESH: Pichia MESH: Base Sequence 01 natural sciences protéine odorante queen pheromone binding protein olfaction antenna sensilla honeybee Pichia pastoris expression Pheromones Pichia law.invention apidae MESH: Bees MESH: Recombinant Proteins law spectrométrie de masse MESH: Gene Expression Regulation Developmental MESH: Insect Proteins MESH: Animals Cloning Molecular odeur électrophorèse 0303 health sciences Sex Characteristics MESH: Pheromones biology General Neuroscience Gene Expression Regulation Developmental Bees Chemoreceptor Cells Recombinant Proteins Cell biology [SDV] Life Sciences [q-bio] Alimentation et Nutrition Recombinant DNA Pheromone Insect Proteins Female [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] MESH: Sex Characteristics Gene isoform MESH: DNA Primers DNA Complementary MESH: Chemoreceptor Cells reine d'abeille Molecular Sequence Data MESH: Sequence Alignment MESH: Carrier Proteins Article Pichia pastoris 03 medical and health sciences insecte social Food and Nutrition Animals MESH: Cloning Molecular [SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] Pheromone binding Amino Acid Sequence phéromone 030304 developmental biology DNA Primers Cloning pichia pastoris MESH: Molecular Sequence Data Base Sequence Sequence Homology Amino Acid Binding protein Neurosciences MESH: DNA Complementary séquence nucléotidique biology.organism_classification Molecular biology MESH: Male 010602 entomology recombinaison Neurons and Cognition Pheromone binding protein Carrier Proteins Sequence Alignment MESH: Female |
| Zdroj: | Journal of Neuroscience Journal of Neuroscience, Society for Neuroscience, 1999, 19 (17), pp.7468-75 Journal of Neuroscience 17 (19), 7468-7475. (1999) Journal of Neuroscience, 1999, 19 (17), pp.7468-75 |
| ISSN: | 0270-6474 1529-2401 |
| Popis: | International audience; Odorant-binding proteins (OBPs) are small abundant extracellular proteins thought to participate in perireceptor events of odor-pheromone detection by carrying, deactivating, and/or selecting odor stimuli. The honeybee queen pheromone is known to play a crucial role in colony organization, in addition to drone sex attraction. We identified, for the first time in a social insect, a binding protein called antennal-specific protein 1 (ASP1), which binds at least one of the major queen pheromone components. ASP1 was characterized by cDNA cloning, expression in Pichia pastoris, and pheromone binding. In situ hybridization showed that it is specifically expressed in the auxiliary cell layer of the antennal olfactory sensilla. The ASP1 sequence revealed it as a divergent member of the insect OBP family. The recombinant protein presented the exact characteristics of the native protein, as shown by mass spectrometry, and N-terminal sequencing and exclusion-diffusion chromatography showed that recombinant ASP1 is dimeric. ASP1 interacts with queen pheromone major components, opposite to another putative honeybee OBP, called ASP2. ASP1 biosynthetic accumulation, followed by nondenaturing electrophoresis during development, starts at day 1 before emergence, in concomitance with the functional maturation of olfactory neurons. The isobar ASP1b isoform appears simultaneously to ASP1a in workers, but only at approximately 2 weeks after emergence in drones. Comparison of in vivo and heterologous expressions suggests that the difference between ASP1 isoforms might be because of dimerization, which might play a physiological role in relation with mate attraction. |
| Databáze: | OpenAIRE |
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