Search results for "odorant-binding proteins"

showing 9 items of 9 documents

The Odorant-Binding Proteins of the Spider Mite Tetranychus urticae

2021

Spider mites are one of the major agricultural pests, feeding on a large variety of plants. As a contribution to understanding chemical communication in these arthropods, we have characterized a recently discovered class of odorant-binding proteins (OBPs) in Tetranychus urticae. As in other species of Chelicerata, the four OBPs of T. urticae contain six conserved cysteines paired in a pattern (C1–C6, C2–C3, C4–C5) differing from that of insect counterparts (C1–C3, C2–C5, C4–C6). Proteomic analysis uncovered a second family of OBPs, including twelve members that are likely to be unique to T. urticae. A three-dimensional model of TurtOBP1, built on the recent X-ray structure of Varroa destruc…

0106 biological sciences0301 basic medicineModels MolecularProteomicsProteomeOdorant bindingProtein ConformationInsectLigandsReceptors Odorant01 natural scienceschemistry.chemical_compoundTetranychus urticaeBiology (General)SpectroscopyPhylogenymedia_commonmass spectrometryGeneticsbiologyligand-bindingMolecular Structurespider mitesGeneral MedicineTetranychus urticaeComputer Science ApplicationsChemistryConiferyl aldehydedisulfide bridgesTetranychidaeProtein Bindingspider mites.QH301-705.5media_common.quotation_subjectodorant-binding proteinsCatalysisArticleInorganic Chemistry03 medical and health sciencesSpider mite<i>Tetranychus urticae</i>AnimalsAmino Acid SequencePhysical and Theoretical ChemistryQD1-999Molecular BiologySpiderOrganic Chemistrybiology.organism_classification010602 entomology030104 developmental biologychemistryVarroa destructorOdorantsChelicerataInternational Journal of Molecular Sciences
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The 40-Year Mystery of Insect Odorant-Binding Proteins

2021

International audience; The survival of insects depends on their ability to detect molecules present in their environment. Odorant-binding proteins (OBPs) form a family of proteins involved in chemoreception. While OBPs were initially found in olfactory appendages, recently these proteins were discovered in other chemosensory and non-chemosensory organs. OBPs can bind, solubilize and transport hydrophobic stimuli to chemoreceptors across the aqueous sensilla lymph. In addition to this broadly accepted “transporter role”, OBPs can also buffer sudden changes in odorant levels and are involved in hygro-reception. The physiological roles of OBPs expressed in other body tissues, such as mouthpar…

0301 basic medicineInsectaChemoreceptorOdorant bindinglcsh:QR1-502Gene ExpressionReviewInsectReceptors OdorantBiochemistryPheromoneslcsh:MicrobiologytasteSexual Behavior Animal0302 clinical medicinemedia_commonbiologyRihanichemosensory functionsArthropod mouthparts3. Good healthCell biologyDrosophila melanogasterodorant-protein-binding assayInsect ProteinsPheromoneDrosophila melanogasterolfactionmedia_common.quotation_subjectK.OlfactionFerveurEvolution Molecularnon-chemosensory functions03 medical and health sciencesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyL. The 40-Year Mystery of Insect Odorant-Binding Proteins insectMolecular BiologyJ.-F.fungiBriandTransporterbiology.organism_classificationodorantprotein-binding assayHematopoiesis030104 developmental biologyinsect[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgeryBiomolecules
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Structure of rat odorant-binding protein OBP1 at 1.6 angstrom resolution

2009

The nasal mucosa is a specialist interfacial region sandwiched between the olfactory system and the gaseous chemical milieu. In mammals and insects, this region is rich in odorant-binding proteins that are thought to aid olfaction by assisting mass transfer of the many different organoleptic compounds that make up the olfactory landscape. However, in mammals at least, our grasp on the exact function of odorant-binding proteins is tentative and better insight into the role of these proteins is warranted, not least because of their apparent significance in the olfactory systems of insects. Here, the crystal structure of rat odorant-binding protein 1 is reported at 1.6 Å resolution. This prote…

Models MolecularOlfactory systemCristallographyProtein ConformationRecombinant Fusion ProteinsMolecular Sequence DataOlfactionOBP1Crystallography X-RayReceptors Odorant010402 general chemistry01 natural sciencesPheromonesPichia pastoris03 medical and health sciences[ CHIM.CRIS ] Chemical Sciences/CristallographyProtein structureSpecies SpecificityStructural BiologyODORANT-BINDING PROTEINS[CHIM.CRIS]Chemical Sciences/CristallographyAnimalsAmino Acid SequencePeptide sequence030304 developmental biology0303 health sciencesBinding SitesSequence Homology Amino AcidbiologyProteinsGeneral MedicineLigand (biochemistry)biology.organism_classificationLipocalinsRatsCristallographie0104 chemical sciencesTransport proteinDNA-Binding ProteinsBiochemistryOdorant-binding proteinbiology.proteinODORANT-BINDING PROTEINS;OBP1Sequence Alignment
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When the nose must remain responsive: glutathione conjugation of the mammary pheromone in the newborn rabbit

2014

In insects, xenobiotic-metabolizing enzymes were demonstrated to regulate pheromones inactivation, clearing them from the olfactory periphery and keeping receptors ready for stimulation renewal. Here, we investigate whether similar processes could occur in mammals, focusing on the pheromonal communication between female rabbits and their newborns. Lactating rabbits emit in their milk a volatile aldehyde, 2-methylbut-2-enal, that elicits searching-grasping in neonates; called the mammary pheromone (MP), it is critical for pups which are constrained to find nipples within the 5 min of daily nursing. For newborns, it is thus essential to remain sensitive to this odorant during the whole nursin…

Vomeronasal organPhysiologyIngénierie des alimentsStimulationPheromonesBehavioral Neurosciencechemistry.chemical_compoundnursingnewbornODORANT-BINDING PROTEINS[SDV.IDA]Life Sciences [q-bio]/Food engineeringDinitrochlorobenzenerabbit (Oryctolagus cuniculus)EXPRESSION PATTERNSAcroleinReceptorGlutathione TransferaseGENE-EXPRESSIONglutathione transferases[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringperireceptor eventsLOCALIZATIONmammary pheromoneGlutathioneSensory SystemsSmellmedicine.anatomical_structureOrgan SpecificitySex pheromonePheromoneFemaleRabbitsENZYMESolfactionmedicine.medical_specialtyOlfactionBiologyNoseGene Expression Regulation EnzymologicPhysiology (medical)Internal medicinemedicineFood engineeringAnimalsLactationAldehydesALDEHYDEGlutathioneFeeding BehaviorUDP-GLUCURONOSYLTRANSFERASEglutathione transferases;mammary pheromone;newborn;nursing;olfaction;perireceptor events;rabbit (Oryctolagus cuniculus);xenobiotic-metabolizing enzymes;RAT OLFACTORY EPITHELIUM;ODORANT-BINDING PROTEINS;S-TRANSFERASE;UDP-GLUCURONOSYLTRANSFERASE;EXPRESSION PATTERNS;VOMERONASAL ORGAN;GENE-EXPRESSION;LOCALIZATION;ALDEHYDE;ENZYMESxenobiotic-metabolizing enzymesRAT OLFACTORY EPITHELIUMS-TRANSFERASENasal MucosaEndocrinologychemistryAnimals NewbornOlfactory epitheliumVOMERONASAL ORGAN
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Rapid odorant release in mammalian odour binding proteins facilitates their temporal coupling to odorant signals.

2010

 ; We have measured the effect of rat odorant-binding protein 1 on the rates of ligand uptake and liquid-to-air transfer rates with a set of defined odorous compounds. Comparison of observed rate constants (k(obs)) with data simulated over a wide range of different kinetic and thermodynamic regimes shows that the data do not agree with the previously held view of a slow off-rate regime (k(off) <0.0004 s(-1)). We propose that a rapid koff would be a necessary requirement for such a system, since slow odorant-release rates would result in significant decorrelation between the olfactory world and odour perception. (c) 2010 Elsevier Ltd. All rights reserved.

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyKineticsAnalytical chemistryOlfactionAcetatesCalorimetryIn Vitro Techniques[ SDV.BA ] Life Sciences [q-bio]/Animal biologyLigandsReceptors OdorantDNA-binding proteinMass Spectrometry03 medical and health sciences0302 clinical medicineReaction rate constantStructural BiologyODORANT-BINDING PROTEINSAnimals[INFO.INFO-BT]Computer Science [cs]/BiotechnologyMolecular Biology030304 developmental biology0303 health sciencesChemistryTemporal couplingLigand[SDV.BA]Life Sciences [q-bio]/Animal biology[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyRecombinant ProteinsRatsSmellKineticsOdorantsBiophysicsOLFACTIONThermodynamics[ INFO.INFO-BT ] Computer Science [cs]/Biotechnology030217 neurology & neurosurgerypsychological phenomena and processesSignal TransductionJournal of molecular biology
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Lipocalins in Arthropod Chemical Communication.

2021

Abstract Lipocalins represent one of the most successful superfamilies of proteins. Most of them are extracellular carriers for hydrophobic ligands across aqueous media, but other functions have been reported. They are present in most living organisms including bacteria. In animals they have been identified in mammals, molluscs, and arthropods; sequences have also been reported for plants. A subgroup of lipocalins, referred to as odorant-binding proteins (OBPs), mediate chemical communication in mammals by ferrying specific pheromones to the vomeronasal organ. So far, these proteins have not been reported as carriers of semiochemicals in other living organisms; instead chemical communicatio…

arthropods; chemical communication; insects; lipocalins; odorant-binding proteins; phylogenesisArthropod AntennaeAcademicSubjects/SCI01140Vomeronasal organProtein familyGenome Insectodorant-binding proteinsphylogenesisLipocalinBiologyarthropodsPheromones03 medical and health sciences0302 clinical medicineGene duplicationGeneticsAnimalsinsectsGeneEcology Evolution Behavior and Systematics030304 developmental biology0303 health sciencesintegumentary systemAcademicSubjects/SCI01130chemical communicationbiology.organism_classificationLipocalinsAnimal CommunicationEvolutionary biologyPhylogenesisSex pheromoneArthropod030217 neurology & neurosurgeryResearch ArticleGenome biology and evolution
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Odorant-binding protein-based optoelectronic tongue and nose for sensing volatile organic compounds

2019

International audience; We developed an array of odorant-binding protein mutants with various binding properties. The same design is suitable for the detection and identification of volatile organic compounds (VOCs) both in the liquid phase and in the gas phase by surface plasmon resonance imaging. The obtained optoelectronic tongue is highly selective at low concentrations of VOCs with a low detection limit, but a narrow linear range. In comparison, the optoelectronic nose gives a much higher signal to noise ratio, but the discrimination of VOCs from different chemical classes requires kinetic data to get rid of non-specific signals. This work shows that these optoelectronic tongue and nos…

electronic nosevolatile organic compoundMaterials scienceElectronic tongueodorant-binding proteins02 engineering and technologyelectronic tongue01 natural sciences[CHIM.ANAL]Chemical Sciences/Analytical chemistrySurface plasmon resonance imaging[CHIM]Chemical SciencesVolatile organic compoundComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationDetection limitElectronic nosebiologybusiness.industry[CHIM.ORGA]Chemical Sciences/Organic chemistry010401 analytical chemistryBinding properties[CHIM.ORGA] Chemical Sciences/Organic chemistry021001 nanoscience & nanotechnology0104 chemical sciences[SDV.AEN] Life Sciences [q-bio]/Food and NutritionchemistryLinear rangeOdorant-binding proteinbiology.proteinOptoelectronicssurface plasmon resonance imaging0210 nano-technologybusiness[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
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Function of odorant-binding proteins in the Drosophila melanogaster chemoreception

2017

National audience; Function of odorant-binding proteins in the Drosophila [i]melanogaster[/i] chemoreception. 18. rencontre du Club de neurobiologie des invertébrés

pichia pastorisanimal structures[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritioneducationodorant-binding proteinsdrosophila melanogasterhumanitiestestingCAFÉ assay[SDV.AEN] Life Sciences [q-bio]/Food and Nutritionprotéineessaiprotein[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionhuman activitiespsychological phenomena and processeshealth care economics and organizationsfluorescent binding assays
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Role of odorant-binding proteins in Drosophila melanogaster chemosensory perception

2019

Chemoperception is used by animals to detect nutritive food and avoid toxic compounds. It also allows animals to identify suitable ecological niche and mating partners. Like many other insects, Drosophila melanogaster possesses a very sensitive chemosensory ability and can detect and discriminate a wide panel of semiochemicals. Chemosensory detection is mostly mediated by olfactory and gustatory systems involving several multigene chemoreceptor families. Volatile and non-volatile chemical compounds entering the sensory organ (sensillum) must be solubilized before being transported through the hydrophilic sensillum lymph bathing the dendrites of chemosensory neurons. These perireceptor event…

tastechemoperception[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biologyperireceptor eventsgoût[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biologyodorant-binding proteinschimioperceptionévénement périrecepteurdrosophilaprotéines de liaison aux odorantsolfaction
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