Evidence of an odorant-binding protein in the human olfactory mucus : location, structural characterization , and odorant-binding properties
| Autor: | Céline Henry, Valérie Bézirard, Jean-Claude Huet, Florence Blon, Jean-Claude Pernollet, Loïc Briand, Didier Trotier, Corinne Eloit, Claude Nespoulous |
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| Přispěvatelé: | Biochimie bactérienne (BIOBAC), Institut National de la Recherche Agronomique (INRA), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL), Université Paris Diderot - Paris 7 (UPD7), ProdInra, Migration |
| Jazyk: | angličtina |
| Rok vydání: | 2002 |
| Předmět: |
Odorant binding
Genetic Vectors Molecular Sequence Data Lipocalin Ligands Receptors Odorant Biochemistry Binding Competitive Pichia ODORANT-BINDING PROPERTIE Pichia pastoris 03 medical and health sciences Olfactory mucosa 0302 clinical medicine Olfactory Mucosa Sequence Analysis Protein medicine [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology Humans Protein Isoforms [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence ODORANT BINDING PROTEIN Peptide sequence ComputingMilieux_MISCELLANEOUS 030304 developmental biology Fluorescent Dyes 0303 health sciences biology Base Sequence Alternative splicing biology.organism_classification Mucus HUMAN OLFACTORY MUCUS Recombinant Proteins Alternative Splicing medicine.anatomical_structure Spectrometry Fluorescence Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Odorants Odorant-binding protein biology.protein Electrophoresis Polyacrylamide Gel 030217 neurology & neurosurgery |
| Zdroj: | Biochemistry Biochemistry, American Chemical Society, 2002, 41 (23), pp.7241-7252 |
| ISSN: | 0006-2960 1520-4995 |
| Popis: | Odorant-binding proteins (OBPs) are small abundant extracellular proteins belonging to the lipocalin superfamily. They are thought to participate in perireceptor events of odor detection by carrying, deactivating, and/or selecting odorant molecules. Putative human OBP genes (hOBP) have recently been described [Lacazette et al. (2000) Hum. Mol. Genet. 9, 289-301], but the presence of the corresponding proteins remained to be established in the human olfactory mucus. This paper reports the first evidence of such expression in the mucus covering the olfactory cleft, where the sensory olfactory epithelium is located. On the contrary, hOBPs were not observed in the nasal mucus covering the septum and the lower turbinate. To demonstrate the odorant binding activity of these proteins, a corresponding recombinant protein variant, hOBP(IIa)(alpha), was secreted by the yeast Pichia pastoris and thoroughly characterized. It appears as a monomer with one disulfide bond located between C59 and C151, a conservative feature of all other vertebrate OBPs. By measuring the displacement of several fluorescent probes, we show that hOBP(IIa)(alpha) is able to bind numerous odorants of diverse chemical structures, with a higher affinity for aldehydes and large fatty acids. A computed 3D model of hOBP(IIa)(alpha) is proposed and reveals that two lysyl residues of the binding pocket may account for the increased affinity for aldehydes. The relatively limited specificity of hOBP(IIa)(alpha) suggests that other human OBPs are expected to take into account the large diversity of odorant molecules. |
| Databáze: | OpenAIRE |
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