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Academic literature on the topic 'Odorant Binding Proteins'

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Published: 4 June 2021
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Journal articles on the topic "Odorant Binding Proteins"

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Pelosi, Paolo. "Odorant-Binding Proteins." Critical Reviews in Biochemistry and Molecular Biology 29, no. 3 (January 1994): 199–228. http://dx.doi.org/10.3109/10409239409086801.

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Sun, Jennifer S., Shuke Xiao, and John R. Carlson. "The diverse small proteins called odorant-binding proteins." Open Biology 8, no. 12 (December 2018): 180208. http://dx.doi.org/10.1098/rsob.180208.

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The term ‘odorant-binding proteins (Obps)’ is used to refer to a large family of insect proteins that are exceptional in their number, abundance and diversity. The name derives from the expression of many family members in the olfactory system of insects and their ability to bind odorants in vitro. However, an increasing body of evidence reveals a much broader role for this family of proteins. Recent results also provoke interesting questions about their mechanisms of action, both within and outside the olfactory system. Here we describe the identification of the first Obps and some cardinal properties of these proteins. We then consider their function, discussing both the prevailing orthodoxy and the increasing grounds for heterodox views. We then examine these proteins from a broader perspective and consider some intriguing questions in need of answers.
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Tegoni, Mariella, Paolo Pelosi, Florence Vincent, Silvia Spinelli, Valérie Campanacci, Stefano Grolli, Roberto Ramoni, and Christian Cambillau. "Mammalian odorant binding proteins." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1482, no. 1-2 (October 2000): 229–40. http://dx.doi.org/10.1016/s0167-4838(00)00167-9.

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Schwartz, Mathieu, Franck Menetrier, Jean-Marie Heydel, Evelyne Chavanne, Philippe Faure, Marc Labrousse, Frédéric Lirussi, et al. "Interactions Between Odorants and Glutathione Transferases in the Human Olfactory Cleft." Chemical Senses 45, no. 8 (August 21, 2020): 645–54. http://dx.doi.org/10.1093/chemse/bjaa055.

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Abstract Xenobiotic metabolizing enzymes and other proteins, including odorant-binding proteins located in the nasal epithelium and mucus, participate in a series of processes modulating the concentration of odorants in the environment of olfactory receptors (ORs) and finely impact odor perception. These enzymes and transporters are thought to participate in odorant degradation or transport. Odorant biotransformation results in 1) changes in the odorant quantity up to their clearance and the termination of signaling and 2) the formation of new odorant stimuli (metabolites). Enzymes, such as cytochrome P450 and glutathione transferases (GSTs), have been proposed to participate in odorant clearance in insects and mammals as odorant metabolizing enzymes. This study aims to explore the function of GSTs in human olfaction. Using immunohistochemical methods, GSTs were found to be localized in human tissues surrounding the olfactory epithelium. Then, the activity of 2 members of the GST family toward odorants was measured using heterologously expressed enzymes. The interactions/reactions with odorants were further characterized using a combination of enzymatic techniques. Furthermore, the structure of the complex between human GSTA1 and the glutathione conjugate of an odorant was determined by X-ray crystallography. Our results strongly suggest the role of human GSTs in the modulation of odorant availability to ORs in the peripheral olfactory process.
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Monte, Massimo Dal, Marisanna Centini, Cecilia Anselmi, and Paolo Pelosi. "Binding of selected odorants to bovine and porcine odorant-binding proteins." Chemical Senses 18, no. 6 (1993): 713–21. http://dx.doi.org/10.1093/chemse/18.6.713.

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Steinbrecht, Rudolf Alexander. "Are Odorant-binding Proteins Involved in Odorant Discrimination?" Chemical Senses 21, no. 6 (1996): 719–27. http://dx.doi.org/10.1093/chemse/21.6.719.

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Moitrier, Lucie, Christine Belloir, Maxence Lalis, Yanxia Hou, Jérémie Topin, and Loïc Briand. "Ligand Binding Properties of Odorant-Binding Protein OBP5 from Mus musculus." Biology 12, no. 1 (December 20, 2022): 2. http://dx.doi.org/10.3390/biology12010002.

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Odorant-binding proteins (OBPs) are abundant soluble proteins secreted in the nasal mucus of a variety of species that are believed to be involved in the transport of odorants toward olfactory receptors. In this study, we report the functional characterization of mouse OBP5 (mOBP5). mOBP5 was recombinantly expressed as a hexahistidine-tagged protein in bacteria and purified using metal affinity chromatography. The oligomeric state and secondary structure composition of mOBP5 were investigated using gel filtration and circular dichroism spectroscopy. Fluorescent experiments revealed that mOBP5 interacts with the fluorescent probe N-phenyl naphthylamine (NPN) with micromolar affinity. Competitive binding experiments with 40 odorants indicated that mOBP5 binds a restricted number of odorants with good affinity. Isothermal titration calorimetry (ITC) confirmed that mOBP5 binds these compounds with association constants in the low micromolar range. Finally, protein homology modeling and molecular docking analysis indicated the amino acid residues of mOBP5 that determine its binding properties.
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PELOSI, PAOLO. "Odorant-Binding Proteins: Structural Aspects." Annals of the New York Academy of Sciences 855, no. 1 OLFACTION AND (November 1998): 281–93. http://dx.doi.org/10.1111/j.1749-6632.1998.tb10584.x.

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Pelosi, Paolo, and Rosario Maida. "Odorant-binding proteins in insects." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 111, no. 3 (July 1995): 503–14. http://dx.doi.org/10.1016/0305-0491(95)00019-5.

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Terrado, Mailyn, Yang Yu, and Erika Plettner. "Correlation of pheromone-binding protein–ligand equilibrium dissociation constants with electroantennogram response patterns." Canadian Journal of Chemistry 96, no. 2 (February 2018): 168–77. http://dx.doi.org/10.1139/cjc-2017-0339.

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Pheromone-binding proteins (PBPs) are water-soluble proteins found at high concentration in the lymph fluid of pheromone-sensing hairs on insect antennae. PBPs could function as pheromone transporters, ferrying the hydrophobic odorants to their cognate odorant receptors. However, it is also possible for these proteins to bind the odorants near the dendritic membrane of pheromone-sensing neurons and, therefore, function as scavengers. The two functions are not mutually exclusive. In this paper, the transporter and (or) scavenger roles of PBPs in pheromone perception were investigated using the pheromone of the gypsy moth (7R, 8S)-epoxy-2-methyloctadecane and analogues with heteroatom (O or S) substitutions in the hydrocarbon chain. PBP–ligand equilibrium dissociation constants (Kd) were correlated with electroantennogram (EAG) response patterns of male gypsy moth antennae to the pheromone, its enantiomer, and their respective analogues. EAG measures the potential drop across the antenna due to odorant receptor activation and subsequent ion channel opening. Three quantifiable properties of the EAG responses were used: lag times from stimulus to response onset, depolarization rates (rate of receptor activation), and repolarization rates (rate of receptor deactivation). Negative correlations were observed between Kd and lag times and between Kd and repolarization rates. Positive correlations were seen with Kd against depolarization rates. The inverse relationship of Kd constants with lag times and the direct relationship with depolarization rates strongly supports transporter function of PBPs. Interestingly, the inverse correlation of Kd constants with repolarization rates suggests a scavenger effect. These results indicate that PBP affects odorant receptor activity through both odorant transport and scavenger functions. Through differences in ligand binding affinities, PBPs influence pheromone availability for receptor activation.
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Dissertations / Theses on the topic "Odorant Binding Proteins"

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Jacobs, Stephen P. "Chemosensory proteins and odorant binding proteins in aphids." Thesis, University of Nottingham, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.435766.

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Cheng, Hui-Yin Patricia. "Towards microarrays of fluorescent odorant binding proteins." Thesis, Imperial College London, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.509508.

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Tuccori, Elena. "Development of biosensors based on Odorant Binding Proteins." Thesis, University of Manchester, 2014. https://www.research.manchester.ac.uk/portal/en/theses/development-of-biosensors-based-on-odorant-binding-proteins(7ce472da-bfbf-4fb0-a0bc-ed61d0d3be49).html.

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This PhD project aimed to investigate the possibility of using Odorant Binding Proteins (OBPs) as sensing layers of chemical sensors, for the detection of organic compounds in both vapour and liquid phases. OBPs are small soluble proteins present in high concentrations in the olfactory system of vertebrates and insects. OBPs are attractive in the biosensor field since they can bind odorants and pheromones in a reversible way. They are resistant to high temperatures and protease activity and they can be easily expressed in large amounts. OBPs belonging to different species of mammals and insects were utilised for developing biosensors relied on different transduction mechanisms. Recombinant OBPs were grafted on the gold electrode of transducers by using Self-assembled monolayers (SAMs) of alkanethiols. The efficiency of the immobilisation method was proved by using electrochemical techniques. Quartz crystal microbalances (QCMs), screen-printed electrodes (SPEs) and interdigitated electrodes (IDEs) were employed for developing three types of OBP-based biosensors. I. QCMs functionalised with OBPs were tested against pheromones (i.e. bombykol and bombykal) and volatile compounds found in foodstuffs (i.e. pyrazine derivatives and geosmin) in vapour phase. The QCM based biosensors showed a good degree of selectivity and a detection limit of the order of parts per billion, in air. II. In liquid phase, impedimetric biosensors based on SPEs also showed a good selectivity and sensitivity being able to detect analyte concentrations of the order of 10-9 M. III. OBPs immobilised on the gold electrodes of IDEs were instead tested against S-(+) carvone vapour, proving that the binding activity of the proteins was preserved in vapour phase and can be quantified as variation of capacitance. The developed OBP biosensors showed good selectivity, sensitivity and stability over time in both liquid and vapour phase. The responses of the sensors were reversible, allowing to the device to be used several times. Moreover, the biosensors were label-free, hence the interaction between OBPs and ligand was directly detected without using auxiliary probes/species. With these findings, we envisage the use of our biosensors in several applications, including monitoring of the quality of food along the transportation and storage, controlling of pests and useful insects in agriculture, or as analytical devices for studying the dynamics in binding processes.
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Rihani, Karen. "Role of odorant-binding proteins in Drosophila melanogaster chemosensory perception." Thesis, Bourgogne Franche-Comté, 2019. http://www.theses.fr/2019UBFCK044.

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La perception des signaux chimiques de l’environnement est un processus nécessaire aux interactions sociales entre les animaux. La Drosophile détecte les molécules odorantes et sapides grâce à ses systèmes gustatif et olfactif impliquant plusieurs familles multigèniques de chimiorécepteurs. Ainsi, ces composés chimiques pénétrant dans l'organe sensoriel (sensille) doivent être solubilisés avant d'être transportés à travers la lymphe sensillaire hydrophile baignant les dendrites des neurones chimiosensoriels. Ces événements périrecepteurs font intervenir plusieurs familles de protéines solubles parmi lesquelles se trouvent les odorant-binding proteins (OBPs). Si les OBPs ont été initialement identifiées dans les sensilles olfactives, certaines sont également exprimées dans les sensilles gustatives. La fonction physiologique des OBPs est encore peu connue mais certaines études révèlent que ces protéines agissent comme transporteurs de molécules lipophiles. Les affinités relativement faibles des OBPs pour les odorants ainsi que leur abondance dans la lymphe sensillaire suggèrent que ces protéines peuvent se lier, solubiliser et transporter des molécules hydrophobes jusqu’aux chimiorécepteurs en traversant la lymphe sensillaire hydrophile. De nouveaux rôles ont été attribués aux OBPs, et en particulier leur capacité à «tamponner» des changements soudains de concentrations d'odorants et leur implication dans la détection de l’humidité. Récemment, l’OBP49a exprimée dans les sensilles gustatives, a été montrée comme étant impliquée dans la détection de certains composés amers. Comme le rôle pérircepteur des OBPs reste encore très peu compris, l'objectif de mon projet de thèse a consisté à clarifier l'implication de certaines OBPs dans l'odorat et le goût chez Drosophila melanogaster. Ma thèse a d’abord consisté à mesurer le rôle des OBPs dans la perception des composés alimentaires chez les adultes D. melanogaster. Les OBPs exprimées dans les appendices gustatifs ont été identifiées par q-PCR et produites en utilisant un système d'expression hétérologue, la levure. Les propriétés de liaison des OBPs recombinantes purifiées ont ensuite été testées pour leur capacité à lier de nombreux ligands potentiels. L’OBP19b est capable de lier certains acides aminés. La cartographie des sensilles et des cellules exprimant l’OBP19b révèle que cette protéine est uniquement exprimée dans certaines cellules accessoires de sensilles précises du labellum. L’OBP19b a été aussi localisée dans le tube digestif et dans certains organes reproducteurs. La comparaison des réponses comportementales et électrophysiologiques sensillaires des mouches témoins et des mouches transgéniques a confirmé que l’OBP19b est impliquée dans la détection de certains acides aminés. De plus, la comparaison des séquences protéique a révélé sa relativement haute conservation au sein des espèces de Drosophilidae et même entre Diptères, ce qui suggère qu’elle joue un rôle crucial vis-à-vis de la recherche de nutriments chez ce groupe d’espèces. J’ai ensuite étudié le rôle de l’OBP28a dans l’olfaction. Cette OBP, l’une des plus abondante dans les antennes de Drosophile, a été montrée importante pour tamponner les variations soudaines de concentrations d'odorants. Des études structurales, génétiques, biochimiques, comportementales et électrophysiologiques ont été réalisées en collaboration avec les membres de l’équipe. L’OBP28a a d'abord été exprimée puis purifiée et sa structure 3D a été résolue. L'étude de ses propriétés de liaison a révélé la capacité de l'OBP28a à se lier à des composés floraux tels que la β-ionone. Les mesures comportementales et électrophysiologiques ont confirmé son rôle physiologique dans la détection de la β-ionone. En conclusion, ma thèse de doctorat met en évidence les rôles nouveaux de deux OBPs dans la chimioréception: l’OBP28a est impliquée dans le détection de molécules florales alors que l’OBP19b est nécessaire pour détecter certains acides aminés
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 events involve a family of soluble proteins named odorant-binding proteins (OBPs). Despite the fact that OBPs were initially found in olfactory sensilla, some OBPs are also expressed in gustatory sensilla. While their physiological roles in olfaction and gustation remain unclear, many studies suggest that OBPs transport lipophilic chemicals. The relatively low affinity of OBPs for odorants and their high abundance in the sensillum lymph both suggest that OBPs can bind, solubilize and transport hydrophobic stimuli to the chemoreceptors across the aqueous sensilla lymph. In addition to this broadly accepted “transporter role” hypothesis, OBPs have also been proposed to buffer sudden changes in odorant levels and to be involved in hygroreception. The role of OBP49a was recently shown in taste: this OBP, expressed in the gustatory system, is required to detect some bitter compounds. However, the role of OBPs in perireceptor events remains largely unknown. The main goal of my thesis project consisted to investigate the involvement of OBPs in the smell and taste sensory modalities using a multi-faceted approach in Drosophila melanogaster.My first research axis consisted to better understand the role of OBPs in the perception of food compounds by using both in vitro and in vivo approaches of OBPs expressed in the gustatory appendages of D. melanogaster adults. After identifying by q-PCR the OBPs expressed in gustatory appendages, we produced them using a heterologous yeast expression system. Then, the binding properties of the recombinant purified OBP were investigated. Our binding assay screen revealed that the taste-expressed OBP19b is able to bind some amino acids. The expression of OBP19b was mapped in specific accessory cells in a subset of proboscis sensilla. This OBP was also expressed in the digestive tract and in some internal reproductive organs. The comparison of behavioural and single-taste sensilla responses between transgenic variants and control flies supported our finding that OBP19b is indeed involved in the detection of some amino acids. Finally, the comparison between various dipteran insects of the OBP19b-like protein coding sequence indicates the relatively high conservation of this protein suggesting its critical role in food search.The second research axis of my PhD thesis focused on the olfactory role of OBP28a. OBP28a was previously shown to be highly expressed in the Drosophila antennae and proposed to buffer quantitative odour variations. To better understand the physiological role of this OBP, and in collaboration with different members of the team, we used structural, genetic, biochemical, behavioural and electrophysiological methods to better understand the role of this OBP. OBP28a was first heterologously expressed and purified. The folding of OBP28a was then determined and the protein was crystallized. The study of the binding properties of OBP28a revealed that it can bind floral compounds such as β-ionone. Behavioural and electrophysiological recordings supported the physiological role of OBP28a in β-ionone detection. In summary, this PhD thesis reveals novel roles of two OBPs in perireceptor chemoreception: OBP28a in the detection of floral compounds and OBP19b in the detection of some amino acids
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Agnihotri, Aniruddha Ravindra. "Molecular study of odorant binding proteins to better understand insect chemosensation." Thesis, Agnihotri, Aniruddha Ravindra (2021) Molecular study of odorant binding proteins to better understand insect chemosensation. PhD thesis, Murdoch University, 2021. https://researchrepository.murdoch.edu.au/id/eprint/65502/.

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Like many other organisms, insects use chemical stimuli to regulate behaviours including feeding, egg-laying, and mating. Odorant binding proteins (OBPs) are one of the crucial components of insect chemosensory system, which play an essential role in transporting the hydrophobic volatile odorant molecules to the olfactory receptors. Most of insect OBPs were investigated by using recombinant technology in bacterial cells due to its fast, cost-effective, and high production mechanism. However, one of the major concerns of bacterial expression system is that the protein is frequently expressed in an unfolded state in inclusion bodies (IBs), which requires further in-vitro protein refolding step to make the protein biologically active. While doing this, there are always high chances of protein misfolding which results in soluble or insoluble protein aggregation. Thus, it is highly important to confirm the efficiency of each refolding method, used for OBP refolding, in terms of getting the correctly folded structure of the target protein. Unfortunately, it was neglected in many previous studies, resulting in significant doubts on various functional studies of insect OBPs. In this study, I used three Helicoverpa armigera OBPs, HarmOBP2, HarmOBP5, and HarmGOBP2, as model proteins to compare the different protein refolding strategies in producing correctly folded recombinant OBPs. Along with that, I have developed a novel pH-dependent method of protein refolding which demonstrated as a more efficient and productive approach for selected HarmOBPs’ refolding compared to other used methods. Further, I also developed a novel reverse chemical ecology method to isolate and identify the candidate natural ligands from host plants for HarmOBPs. This study points out a crucial but largely ignored step of insect OBP research, protein refolding and the loopholes associated with it in previous studies, which will improve our understanding of insect chemosensation and help develop more efficient and environmentally friendly insect control strategies.
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Foret, Sylvain, and sylvain foret@anu edu au. "Function and Evolution of Putative Odorant Carriers in the Honey Bee (Apis mellifera)." The Australian National University. Research School of Biological Sciences, 2007. http://thesis.anu.edu.au./public/adt-ANU20070613.144745.

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The remarkable olfactory power of insect species is thought to be generated by a combinatorial action of G-protein-coupled olfactory receptors (ORs) and olfactory carriers. Two such carrier gene families are found in insects: the odorant binding proteins (OBPs) and the chemosensory proteins (CSPs). In olfactory sensilla, OBPs and CSPs are believed to deliver hydrophobic air-borne molecules to ORs, but their expression in non-olfactory tissues suggests that they also may function as general carriers in other developmental and physiological processes. ¶ Bioinformatics and experimental approaches were used to characterise the OBP and CSP gene families in a highly social insect, the western honey bee (Apis mellifera). Comparison with other insects reveals that the honey bee has the smallest set of these genes, consisting of only 21 OBPs and 6 CSPs. These numbers stand in stark contrast to the 66 OBPs and 7 CSPs in the mosquito Anopheles gambiae and the 46 OBPs and 20 CSPs in the beetle Tribolium castaneum. The genes belonging to both families are often organised in clusters, and evolve by lineage specic expansions. Positive selection has been found to play a role in generating a greater sequence diversication in the OBP family in contrast to the CSP gene family that is more conserved, especially in the binding pocket. Expression proling under a wide range of conditions shows that, in the honey, bee only a minority of these genes are antenna-specic. The remaining genes are expressed either ubiquitously, or are tightly regulated in specialized tissues or during development. These findings support the view that OBPs and CSPs are not restricted to olfaction, and are likely to be involved in broader physiological functions. ¶ Finally, the detailed expression study and the functional characterization of a member of the CSP family, uth (unable-to-hatch), is reported. This gene is expressed in a maternal-zygotic fashion, and is restricted to the egg and embryo. Blocking the zygotic expression of uth with double-stranded RNA causes abnormalities in all body parts where this gene is highly expressed. The treated embryos are `unable-to-hatch' and cannot progress to the larval stages. Our ndings reveal a novel, essential role for this gene family and suggest that uth is an ectodermal gene involved in embryonic cuticle formation.
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Maïbèche-Coisné, Martine. "Etudes structurale et fonctionnelle des odorant-binding proteins chez la noctuelle mamestra brassicae l. (lepidoptera : noctuidea)." Paris 6, 1997. http://www.theses.fr/1997PA066126.

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L'olfaction est un des modes sensoriels predominant chez les lepidopteres crepusculaires et nocturnes, et ces animaux s'averent un modele de choix pour l'etude des mecanismes moleculaires de la reception des signaux olfactifs et de leur transduction vers des niveaux superieurs d'integration. Depuis leur decouverte dans le systeme olfactif peripherique des insectes et des vertebres, le degre d'implication des odorant-binding proteins (obp) dans les processus de discrimination des odeurs n'est toujours pas elucide. Dans ce cadre, nous avons entrepris l'etude de telles proteines chez la noctuelle du chou mamestra brassicae l. , ravageur des cultures dont le systeme de communication chimique est bien connu. L'utilisation combinee de differentes techniques biochimiques et immunologiques nous a permis de caracteriser et de purifier plusieurs proteines de type pbp (pheromone-binding protein) et gobp (general odorant-binding protein) dans les antennes des males et des femelles. Cette microdiversite est en faveur d'une participation active de ces proteines dans le tri des molecules odorantes. L'etude fonctionnelle de ces proteines a ete effectuee, en utilisant des proteines purifiees et le compose majoritaire de la pheromone sexuelle femelle tritie. Ce compose est fixe de facon specifique par la proteine pbp qui est la plus abondante dans les extraits antennaires males, et il peut egalement etre fixe par les pbp de la femelle. Ces resultats montrent la specificite de l'interaction proteine-compose pheromonal et confortent l'hypothese selon laquelle seul le complexe specifique entre une proteine et son ligand serait capable d'activer le recepteur olfactif. L'utilisation de la biologie moleculaire a permis de cloner les genes codant differentes pbp et une gobp chez le male, et il a ete possible de correler les proprietes fonctionnelles de ces differentes proteines avec des differences dans leur structure primaire. Notamment, des variations localisees dans le site potentiel de fixation des molecules odorantes pourraient expliquer l'affinite opposee de deux des pbp du male envers le compose pheromonal majoritaire. L'etude de la structure et de l'expression des genes correspondant a ete initiee et l'expression preliminaire d'une proteine de type gobp recombinante a ete effectuee dans un systeme procaryote. L'objectif vise par la production de proteines recombinantes est d'en etudier la structure tridimensionnelle, encore inconnue chez les insectes. L'ensemble de ces resultats apportent une meilleure comprehension des mecanismes moleculaires du codage des odeurs pheromonales chez m. Brassicae. Ils permettent d'attribuer aux pbp un role de filtre vis-a-vis des molecules odorantes, et dans l'hypothese de l'activation du recepteur par le complexe pbp-pheromone, un role protecteur a l'egard du recepteur olfactif.
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Manoharan, Malini. "Genomic, structural and functional characterization of odorant binding proteins in olfaction of mosquitoes involved in infectious disease transmission." Phd thesis, Université de la Réunion, 2011. http://tel.archives-ouvertes.fr/tel-00979587.

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The role of odorant binding proteins in the olfaction of mosquitoes, the primary mechanism of human host recognition, has been an important focus of biological research in the field of infectious disease transmission by these insects. This thesis provides an in depth knowledge of these proteins in three mosquito species Anopheles gambiae, Aedes aegypti and Culex quinquefasciatus. A large scale analysis on these genomes has been carried out towards the identification of the odorant binding proteins in the mosquito genomes. Identification of many new OBP members, in particular in the Aedes aegypti and Culex quinquefasciatus species, and an extensive phylogenetic analysis presenting a novel classification of the OBP subfamilies of these mosquito species has been proposed. This results further demonstrates the extraordinary multiplicity and diversity of the OBP gene repertoire in these three mosquito genomes and highlights the striking sequence features that are nevertheless highly conserved across all mosquito OBPs. Owing to the availability of homologous structures from mosquitoes or related species, the 3D structure modelling of all the Classic OBPs from the three genomes (representing in total 137 structures) has been performed. This was completed by large scale docking studies on these structures by screening a large set of compounds that are known to be mosquito attractants or repellents. These provide many exciting new insights into the structural and functional aspects towards understanding the efficacy of some repellents and of some attractants from human emanations. Through molecular dynamics simulation, the structural changes observed in an OBP bounded to an odorant when pH conditions are modified were characterized and the probable mechanism of ligand binding and release is presented. This work provides the first insights to many of the long awaited questions on the genomic, structural and functional characterization of mosquito OBPs and can be viewed as a reliable starting point for further experimental research focussed on these aspects.
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Rojas, Gallardo Diana Marcela. "Evolução molecular da família gênica dos receptores de odores e proteínas ligantes a feromônios e genética de populações de genes quimiossensoriais em espécies de Anastrepha do grupo fraterculus." Universidade Federal de São Carlos, 2016. https://repositorio.ufscar.br/handle/ufscar/8773.

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This dissertation is divided into three chapters. In the first chapter, we provide a concise literature review that discusses key theoretical concepts, the rationale, and main objectives outlined for this study. The second chapter investigates the molecular evolution of the gene family of odor receptors (ORs) identified in the transcriptomes of two species of fruit flies of great economic importance: Anastrepha fraterculus and A. obliqua. The results showed a high percentage of average identities between ORs from these species, as well as recent gene expansions with signs of positive selection. A comparison of rates of synonymous and nonsynonymous substitutions among Anastrepha species detected evidence of positive selection in the gene Or7c, which is associated to an important potential role in aggregation behavior and host choice for oviposition in D. melanogaster. The third chapter investigates patterns of molecular evolution in pheromone binding proteins (PBPs), also identified in A. fraterculus and A. obliqua, as well as studied pattern of polymorphisms, divergence and populational structure of four chemosensory genes amplified in four species of tephritid flies of fraterculus group: A. fraterculus, A. obliqua, A. sororcula and A. turpiniae. This study contrasted previously identified genes with evidence of positive and purifying selection in order to investigate whether they are contributing to the differentiation among some of the species of this group. We found no evidence of positive selection in PBPs studied in a more global comparison, although we found positive selection signals in some of the genes and studied strains. Population analysis of chemosensory genes in different species of Anastrepha detected high levels of intraspecific nucleotide and haplotype diversity. Divergence tests showed that A. obliqua is the most different species of the ones here investigated, having, in general, high levels of nucleotide substitutions, non-synonymous divergence, as well as fixed species specific differences, whereas we failed to find similar differences amongst the other species here studied. The genes Obp28a, Or7c and Or7d were differentiated in A. obliqua, indicating a potential role in the differentiation of other species in the group, or in this species’ diversification and adaptation.
A presente dissertação encontra-se dividida em três capítulos. O primeiro capítulo apresenta uma concisa revisão bibliográfica que aborda os principais conceitos teóricos, a justificativa e os objetivos delineados para este estudo. O segundo capítulo apresenta um estudo da evolução molecular da família gênica dos receptores de odores (ORs) identificados nos transcriptomas de duas espécies de moscas-das-frutas de grande importância econômica: Anastrepha fraterculus e A.obliqua. Os resultados mostraram uma alta porcentagem de identidade média entre os ORs destas espécies, assim como expansões gênicas recentes com sinal de seleção positiva. Quando comparamos as taxas de substituições sinônimas e não-sinônimas entre as espécies de Anastrepha encontramos evidências de seleção positiva no gene Or7c, que está associado em D. melanogaster a um potencial importante papel nos comportamentos de agregação e escolha de frutos para oviposição. No terceiro capítulo apresentamos um estudo do padrão de evolução molecular dos genes que codificam para proteínas ligantes aos feromônios (PBPs), também identificados em A. fraterculus e A. obliqua, assim como também estudamos o padrão de polimorfismos, divergência e estrutura dos genes quimiossensoriais Obp28a, Obp84a, Or7c e Or7d os quais foram amplificados em quatro espécies de moscas-das-frutas do grupo fraterculus, A. fraterculus, A. obliqua, A. sororcula e A. turpiniae. Este estudo foi realizado contrastando genes identificados com sinais de seleção positiva e seleção purificadora com o intuito de investigar se eles estão contribuindo para a diferenciação entre algumas das espécies desse grupo. Não encontramos evidências de seleção positiva nas PBPs estudadas em uma comparação mais global, embora tenhamos encontrado sinais de seleção positiva em alguns dos genes e linhagens estudadas. A análise populacional de genes quimiossensoriais em diferentes espécies de Anastrepha detectou níveis altos de diversidade nucleotídica e haplotípica dentro das espécies. Os testes de divergência mostraram que a espécie A. obliqua é a espécie mais diferenciada, apresentando, em geral, altos níveis de substituições nucleotídicas, divergência não-sinônima, assim como diferenças fixadas quando comparada com as outras espécies. Os genes Obp28a, Or7c e Or7d mostraram-se diferenciados em A. obliqua, indicando um potencial papel na diferenciação desta espécie com respeito às outras espécies estudadas.
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Bunyarataphan, Sasinee. "Biosensors based on bovine odorant binding protein (bOBP)." Thesis, Imperial College London, 2013. http://hdl.handle.net/10044/1/11053.

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Recombinant bovine odorant binding protein (bOBP) is a very promising platform for building protein-based biosensors. The protein possesses a broad binding specificity for hydrophobic molecules with affinities in the sub-micromolar range. Previous work has shown non-covalent binding of 1-aminoanthracene (1-AMA) in the internal cavities of bOBP that results in a large enhancement of fluorescence intensity. We have shown fluorescence titrations of recombinant bOBP with 1-AMA yielded a single type of binding site with a Kd of 0.16 ± 0.023 μM. Competitive displacement assays between 1-AMA and other ligands such as thymol were established and the results indicated their binding to bOBP. The strategy of competitive binding with 1-AMA was thus employed to quantify thymol concentration for the bOBP biosensors. Ten different solid supports for the bOBP biosensors were examined for their biocompatibility with bOBP function using 1-AMA as a probe. The result was that nitrocellulose was chosen as the best membrane for immobilization, probably due to its 3-D micro-porous matrix (sponge structure) that provides a much larger surface area for protein binding compared with 2-D surfaces. It was found that the optimum operating concentrations of bOBP and 1-AMA and the method for the immobilization was incubation of nitrocellulose with the complex of 100μM bOBP and 100μM 1-AMA solution. The amounts of the total and functional protein binding to nitrocellulose were 7 ± 0.1 and 7 ± 0.4 nmol bOBP per cm2 of membrane, respectively. A fibre-optic biosensor based on bOBP has therefore been constructed. It has been an extrinsic sensor with bOBP immobilized on a nitrocellulose membrane placed at the tip of a probe of a bifurcated fibre-optic bundle that was in turn connected to the LLS-385 LED light source and the HR2000 spectrometer. The light emitted by fluorescent 1-AMA bound bOBP was detected by 2048-element CCD array of the spectrometer. The LODs for thymol in the liquid phase were found to be 14 ± 6 μM (calculated as S/N = 3), which is less than the guideline values considered to be toxic to humans. Moreover, this fibre-optic bOBP biosensor was also capable of sensing thymol vapour, and some potential uses of this sensor will be described.
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Books on the topic "Odorant Binding Proteins"

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Derek, Chadwick, Marsh Joan, Goode Jamie, and Symposium on the Molecular Basis of Smell and Taste Transduction (1993 : London, England), eds. The Molecular basis of smell and taste transduction. Chichester: Wiley, 1993.

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Odorant Binding and Chemosensory Proteins. Elsevier, 2020. http://dx.doi.org/10.1016/s0076-6879(20)x0014-0.

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Pelosi, Paolo, and Wolfgang Knoll. Odorant Binding and Chemosensory Proteins. Elsevier Science & Technology, 2020.

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Pelosi, Paolo, and Wolfgang Knoll. Odorant Binding and Chemosensory Proteins. Elsevier Science & Technology Books, 2020.

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Goode, Jamie A., Joan Marsh, and Derek J. Chadwick. Molecular Basis of Smell and Taste Transduction. Wiley & Sons, Incorporated, John, 2008.

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Book chapters on the topic "Odorant Binding Proteins"

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Steinbrecht, R. A., M. Laue, S. G. Zhang, and G. Ziegelberger. "Immunocytochemistry of Odorant-Binding Proteins." In Olfaction and Taste XI, 804–7. Tokyo: Springer Japan, 1994. http://dx.doi.org/10.1007/978-4-431-68355-1_327.

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Persaud, Krishna C., and Elena Tuccori. "Biosensors Based on Odorant Binding Proteins." In Bioelectronic Nose, 171–90. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-8613-3_10.

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Lu, Yanli, Yao Yao, and Qingjun Liu. "Smell Sensors Based on Odorant Binding Proteins." In Bioinspired Smell and Taste Sensors, 129–44. Dordrecht: Springer Netherlands, 2015. http://dx.doi.org/10.1007/978-94-017-7333-1_7.

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Steinbrecht, R. A., M. Laue, R. Maida, and G. Ziegelberger. "Odorant-binding proteins and their role in the detection of plant odours." In Proceedings of the 9th International Symposium on Insect-Plant Relationships, 15–18. Dordrecht: Springer Netherlands, 1996. http://dx.doi.org/10.1007/978-94-009-1720-0_3.

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Ozaki, Mamiko. "Odorant-Binding Proteins in Taste System: Putative Roles in Taste Sensation and Behavior." In Olfactory Concepts of Insect Control - Alternative to insecticides, 187–204. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-05165-5_8.

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Capone, S., C. De Pascali, L. Francioso, P. Siciliano, K. C. Persaud, and A. M. Pisanelli. "Odorant Binding Proteins as Sensing Layers for Novel Gas Biosensors: An Impedance Spectroscopy Characterization." In Lecture Notes in Electrical Engineering, 317–24. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-1324-6_49.

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Pelosi, P., C. Maremmani, and A. Muratorio. "Purification of an Odorant Binding Protein from Human Nasal Mucosa." In Chemosensory Information Processing, 125–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-75127-1_9.

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Di Pietrantonio, F., I. Zaccari, M. Benetti, D. Cannatà, E. Verona, R. Crescenzo, V. Scognamiglio, and S. D’Auria. "Surface Acoustic Wave Biosensor Based on a Recombinant Bovine Odorant-Binding Protein." In Lecture Notes in Electrical Engineering, 201–5. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3606-3_38.

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Gaubert, Anaïs, Béatrice Amigues, Silvia Spinelli, and Christian Cambillau. "Structure of odorant binding proteins and chemosensory proteins determined by X-ray crystallography." In Odorant Binding and Chemosensory Proteins, 151–67. Elsevier, 2020. http://dx.doi.org/10.1016/bs.mie.2020.04.070.

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Scaloni, Andrea. "Analysis of post-translational modifications in soluble proteins involved in chemical communication from mammals and insects." In Odorant Binding and Chemosensory Proteins, 103–24. Elsevier, 2020. http://dx.doi.org/10.1016/bs.mie.2020.04.062.

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Conference papers on the topic "Odorant Binding Proteins"

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Cali, Khasim, Emmanuel Scorsone, and Krishna Persaud. "Odorant binding proteins based sniffing device for detection of tobacco." In 2017 ISOCS/IEEE International Symposium on Olfaction and Electronic Nose (ISOEN). IEEE, 2017. http://dx.doi.org/10.1109/isoen.2017.7968918.

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Zoumpoulakis, Panagiotis, Eftichia Kritsi, and Spyros Zographos. "New Hit Compounds Targeting Odorant Binding Proteins (OBPs) as Putative Repellents." In 3rd International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2017. http://dx.doi.org/10.3390/ecmc-3-04658.

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Di Pietrantonio, Fabio, Massimiliano Benetti, Domenico Cannata, Antonio Varriale, Sabato D'Auria, Alexandra Palla-Papavlu, Pere Serra, and Enrico Verona. "Surface acoustic wave biosensor based on odorant binding proteins deposited by laser induced forward transfer." In 2013 IEEE International Ultrasonics Symposium (IUS). IEEE, 2013. http://dx.doi.org/10.1109/ultsym.2013.0548.

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Possas-Abreu, Maira, Lionel Rousseau, Farbod Ghassemi, Gaelle Lissorgues, Massiel Habchi, Emmanuel Scorsone, Khasim Cal, and Krishna Persaud. "Biomimetic diamond MEMS sensors based on odorant-binding proteins: Sensors validation through an autonomous electronic system." In 2017 ISOCS/IEEE International Symposium on Olfaction and Electronic Nose (ISOEN). IEEE, 2017. http://dx.doi.org/10.1109/isoen.2017.7968909.

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Balakrishnan, Karthi. "RNAi knockdown of red flour beetle, Tribolium castaneum, odorant binding proteins result in altered electrophysiological responses." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.114307.

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Tuccori, Elena, and Krishna C. Persaud. "Pheromone Detection Using Odorant Binding Protein Sensors." In 2019 IEEE International Symposium on Olfaction and Electronic Nose (ISOEN). IEEE, 2019. http://dx.doi.org/10.1109/isoen.2019.8823345.

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Yi, Jiankun. "Wild type and mutated odorant binding protein fromAnopheles funestus differ in binding properties." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.113903.

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Capone, S., C. De Pascali, L. Francioso, P. Siciliano, K. C. Persaud, and A. M. Pisanelli. "Electrical characterization of a pig odorant binding protein by Impedance Spectroscopy." In 2009 IEEE Sensors. IEEE, 2009. http://dx.doi.org/10.1109/icsens.2009.5398471.

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Northey, Tom. "Crystal structures and binding dynamics of odorant-binding protein 3 from two aphid speciesMegoura viciaeandNasonovia ribisnigri." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.110369.

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Hurot, Charlotte, Arnaud Buhot, Emilie Barou, Christine Belloir, Loic Briand, and Yanxia Hou. "Odorant-binding protein-based optoelectronic tongue and nose for sensing volatile organic compounds." In 2019 IEEE International Symposium on Olfaction and Electronic Nose (ISOEN). IEEE, 2019. http://dx.doi.org/10.1109/isoen.2019.8823179.

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