Academic literature on the topic 'Chemosensory proteins'

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Journal articles on the topic "Chemosensory proteins"

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Randazzo, B., F. Abbate, E. Ciriaco, G. Montalbano, M. F. Madrigrano, and M. B. Levanti. "Chemosensory proteins in the chemosensory organs of adult zebrafish." Annals of Anatomy - Anatomischer Anzeiger 207 (September 2016): 125. http://dx.doi.org/10.1016/j.aanat.2016.04.024.

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Ban, L., A. Scaloni, A. Brandazza, S. Angeli, L. Zhang, Y. Yan, and Paolo Pelosi. "Chemosensory proteins of Locusta migratoria." Insect Molecular Biology 12, no. 2 (April 2003): 125–34. http://dx.doi.org/10.1046/j.1365-2583.2003.00394.x.

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Rondoni, Gabriele, Alessandro Roman, Camille Meslin, Nicolas Montagné, Eric Conti, and Emmanuelle Jacquin-Joly. "Antennal Transcriptome Analysis and Identification of Candidate Chemosensory Genes of the Harlequin Ladybird Beetle, Harmonia axyridis (Pallas) (Coleoptera: Coccinellidae)." Insects 12, no. 3 (March 2, 2021): 209. http://dx.doi.org/10.3390/insects12030209.

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In predatory ladybirds (Coleoptera: Coccinellidae), antennae are important for chemosensory reception used during food and mate location, and for finding a suitable oviposition habitat. Based on NextSeq 550 Illumina sequencing, we assembled the antennal transcriptome of mated Harmonia axyridis (Pallas) (Coleoptera: Coccinellidae) males and females and described the first chemosensory gene repertoire expressed in this species. We annotated candidate chemosensory sequences encoding 26 odorant receptors (including the coreceptor, Orco), 17 gustatory receptors, 27 ionotropic receptors, 31 odorant-binding proteins, 12 chemosensory proteins, and 4 sensory neuron membrane proteins. Maximum-likelihood phylogenetic analyses allowed to assign candidate H. axyridis chemosensory genes to previously described groups in each of these families. Differential expression analysis between males and females revealed low variability between sexes, possibly reflecting the known absence of relevant sexual dimorphism in the structure of the antennae and in the distribution and abundance of the sensilla. However, we revealed significant differences in expression of three chemosensory genes, namely two male-biased odorant-binding proteins and one male-biased odorant receptor, suggesting their possible involvement in pheromone detection. Our data pave the way for improving the understanding of the molecular basis of chemosensory reception in Coccinellidae.
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Segura-León, Obdulia L., Brenda Torres-Huerta, Alan Rubén Estrada-Pérez, Juan Cibrián-Tovar, Fidel de la Cruz Hernandez-Hernandez, José Luis Cruz-Jaramillo, José Salvador Meza-Hernández, and Fabian Sánchez-Galicia. "Identification of Candidate Chemosensory Gene Families by Head Transcriptomes Analysis in the Mexican Fruit Fly, Anastrepha ludens Loew (Diptera: Tephritidae)." International Journal of Molecular Sciences 23, no. 18 (September 11, 2022): 10531. http://dx.doi.org/10.3390/ijms231810531.

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Insect chemosensory systems, such as smell and taste, are mediated by chemosensory receptor and non-receptor protein families. In the last decade, many studies have focused on discovering these families in Tephritidae species of agricultural importance. However, to date, there is no information on the Mexican fruit fly Anastrepha ludens Loew, a priority pest of quarantine importance in Mexico and other countries. This work represents the first effort to identify, classify and characterize the six chemosensory gene families by analyzing two head transcriptomes of sexually immature and mature adults of A. ludens from laboratory-reared and wild populations, respectively. We identified 120 chemosensory genes encoding 31 Odorant-Binding Proteins (OBPs), 5 Chemosensory Proteins (CSPs), 2 Sensory Neuron Membrane Proteins (SNMPs), 42 Odorant Receptors (ORs), 17 Ionotropic Receptors (IRs), and 23 Gustatory Receptors (GRs). The 120 described chemosensory proteins of the Mexican fruit fly significantly contribute to the genetic databases of insects, particularly dipterans. Except for some OBPs, this work reports for the first time the repertoire of olfactory proteins for one species of the genus Anastrepha, which provides a further basis for studying the olfactory system in the family Tephritidae, one of the most important for its economic and social impact worldwide.
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Kang, Z. W., F. H. Liu, R. P. Pang, W. B. Yu, X. L. Tan, Z. Q. Zheng, H. G. Tian, and T. X. Liu. "The identification and expression analysis of candidate chemosensory genes in the bird cherry-oat aphid Rhopalosiphum padi (L.)." Bulletin of Entomological Research 108, no. 5 (December 4, 2017): 645–57. http://dx.doi.org/10.1017/s0007485317001171.

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AbstractThe bird cherry-oat aphid Rhopalosiphum padi (L.) is one of the most important wheat pests with polyphagia and autumn migrants. And, chemosensory genes were thought to play a key role in insect searching their hosts, food and mate. However, a systematic identification of the chemosensory genes in this pest has not been reported. Thus, in this study, we identified 14 odorant-binding proteins, nine chemosensory proteins, one sensory neuron membrane protein, 15 odorant receptors, 19 gustatory receptors and 16 ionotropic receptors from R. padi transcriptomes with a significantly similarity (E-value < 10−5) to known chemosensory genes in Acyrthosiphon pisum and Aphis gossypii. In addition, real-time quantitative polymerase chain reaction (RT-qPCR) was employed to determine the expression profiles of obtained genes. Among these obtained genes, we selected 23 chemosensory genes to analyze their expression patterns in different tissues, wing morphs and host plants. We found that except RpOBP1, RpOBP3, RpOBP4 and RpOBP5, the rest of the selected genes were highly expressed in the head with antennae compared with body without head and antennae. Besides that, the stimulation and depression of chemosensory genes by plant switch indicated that chemosensory genes might be involved in the plant suitability assessment. These results not only provide insights for the potential roles of chemosensory genes in plant search and perception of R. padi but also provide initial background information for the further research on the molecular mechanism of the polyphagia and autumn migrants of it. Furthermore, these chemosensory genes are also the candidate targets for pest management control in future.
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Liu, Xiaolong, Na Tong, Zheran Wu, Yang Li, Meiqi Ma, Pei Liu, and Min Lu. "Identification of Chemosensory Genes Based on the Antennal Transcriptomic Analysis of Plagiodera versicolora." Insects 13, no. 1 (December 29, 2021): 36. http://dx.doi.org/10.3390/insects13010036.

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Insects can sense surrounding chemical signals by their accurate chemosensory systems. This system plays a vital role in the life history of insects. Several gene families participate in chemosensory processes, including odorant receptors (ORs), ionotropic receptors (IRs), gustatory receptors (GRs), chemosensory proteins (CSPs), odorant binding proteins (OBPs), and sensory neuron membrane proteins (SNMPs). Plagiodera versicolora (Coleoptera: Chrysomelidae), is a leaf-eating forest pest found in salicaceous trees worldwide. In this study, a transcriptome analysis of male and female adult antennae in P. versicolora individuals was conducted, which identified a total of 98 candidate chemosensory genes including 40 ORs, 7 IRs, 13 GRs, 10 CSPs, 24 OBPs, and 4 SNMPs. Subsequently, the tissue expression profiles of 15 P. versicolora OBPs (PverOBPs) and 39 ORs (PverORs) were conducted by quantitative real-time PCR. The data showed that almost all PverOBPs and PverORs were highly expressed in the male and female antennae. In addition, several OBPs and ORs (PverOBP10, PverOBP12, PverOBP18, PverOR24, and PverOR35) had higher expression levels in female antennae than those in the male antennae, indicating that these genes may be taking part in some female-specific behaviors, such as find mates, oviposition site, etc. This study deeply promotes further understanding of the chemosensory system and functional studies of the chemoreception genes in P. versicolora.
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Pelosi, P. "Diversity of Odorant-binding Proteins and Chemosensory Proteins in Insects." Chemical Senses 30, Supplement 1 (January 1, 2005): i291—i292. http://dx.doi.org/10.1093/chemse/bjh229.

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Mameli, Marina, Andrea Tuccini, Mario Mazza, Ruggero Petacchi, and Paolo Pelosi. "Soluble proteins in chemosensory organs of phasmids." Insect Biochemistry and Molecular Biology 26, no. 8-9 (September 1996): 875–82. http://dx.doi.org/10.1016/s0965-1748(96)00055-0.

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Picimbon, Jean-François, Karen Dietrich, Heinz Breer, and Jürgen Krieger. "Chemosensory proteins of Locusta migratoria (Orthoptera: Acrididae)." Insect Biochemistry and Molecular Biology 30, no. 3 (March 2000): 233–41. http://dx.doi.org/10.1016/s0965-1748(99)00121-6.

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Agnihotri, Aniruddha, Naiyong Liu, and Wei Xu. "Chemosensory Proteins (CSPs) in the Cotton Bollworm Helicoverpa armigera." Insects 13, no. 1 (December 27, 2021): 29. http://dx.doi.org/10.3390/insects13010029.

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Chemosensory proteins (CSPs) are a family of small, soluble proteins that play a crucial role in transporting odorant and pheromone molecules in the insect chemosensory system. Recent studies reveal that they also function in development, nutrient metabolism and insecticide resistance. In-depth and systematic characterization of previously unknown CSPs will be valuable to investigate more detailed functionalities of this protein family. Here, we identified 27 CSP genes from the genome and transcriptome sequences of cotton bollworm, Helicoverpa armigera (Hübner). The expression patterns of these genes were studied by using transcriptomic data obtained from different tissues and stages. The results demonstrate that H. armigera CSP genes are not only highly expressed in chemosensory tissues, such as antennae, mouthparts, and tarsi, but also in the salivary glands, cuticle epidermis, and hind gut. HarmCSP6 and 22 were selected as candidate CSPs for expression in Escherichia coli and purification. A new method was developed that significantly increased the HarmCSP6 and 22 expression levels as soluble recombinant proteins for purification. This study advances our understanding of insect CSPs and provides a new approach to highly express recombinant CSPs in E. coli.
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Dissertations / Theses on the topic "Chemosensory 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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Mantotta, Jeevani Charika. "Analysis of chemosensory proteins in Rhodobacter sphaeroides." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249546.

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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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Chiu, Sheng-Wen. "Spatiotemporal dynamics of cytoskeletal and chemosensory proteins in the bacterium Rhodobacter sphaeroides." Thesis, University of Oxford, 2014. http://ora.ox.ac.uk/objects/uuid:d7d05b1a-07c5-4e26-9650-37bcfae2fade.

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The discovery of the prokaryotic cytoskeleton has revolutionized our thinking about spatial organisation in prokaryotes. However, the roles different bacterial cytoskeletal proteins play in the localisations of diverse biomolecules are controversial. Bacterial chemotaxis depends on signalling through large protein clusters and each cell must inherit a cluster on cytokinesis. In Escherichia coli the membrane chemosensory clusters are polar and new static clusters form at pre-cytokinetic sites, ensuring positioning at new poles after cytokinesis and suggesting a role for the bacterial FtsZ and MreB cytoskeletons. Rhodobacter sphaeroides has both polar, membrane-associated and cytoplasmic, chromosome-associated chemosensory clusters. This study sought to investigate the roles of FtsZ and MreB in the partitioning of the two chemosensory clusters in R. sphaeroides. The relative positioning between the two chemosensory systems, FtsZ and MreB in R. sphaeroides cells during the cell cycle was monitored using fluorescence microscopy. FtsZ forms polar spots after cytokinesis, which redistribute to the midcell forming nodes from which gradients of FtsZ extend circumferentially to form the Z-ring. The proposed node-precursor model might represent a common mechanism for the formation of cytokinetic rings. The MreB cytoskeleton continuously reorganizes between patchy and filamentous structures, and colocalises with FtsZ at midcell. Membrane chemosensory proteins form individual dynamic unit-clusters with mature clusters containing about 1000 CheW3 proteins. These unit-clusters diffuse randomly within the membrane but have a higher propensity for curved regions like cell poles. Membrane clusters do not colocalise with FtsZ and MreB and appear excluded from the Z-ring vicinity. The bipolar localisation of membrane clusters is established after cell division via random diffusion and polar trapping of clusters. The cytoplasmic chemosensory clusters colocalise with FtsZ at midcell in new-born cells. Before cytokinesis one cluster moves to a daughter cell, followed by the second moving to the other cell. FtsZ and MreB do not participate in the positioning of cytoplasmic clusters. Therefore the two homologous chemosensory clusters use different mechanisms to ensure partitioning, and neither system utilizes FtsZ or MreB for positioning.
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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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Souleymane, Diallo. "Coding of tsetse repellents by olfactory sensory neurons: towards the improvement and the development of novel tsetse repellents." University of Western Cape, 2021. http://hdl.handle.net/11394/8039.

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Philosophiae Doctor - PhD
Tsetse flies are the biological vectors of human and animal trypanosomiasis and hence representant medical and veterinary importance. The sense of smell plays a significant role in tsetse and its ecological interaction, such as finding blood meal source, resting, and larvicidal sites and for mating. Tsetse olfactory behaviour can be exploited for their management; however, olfactory studies in tsetse flies are still fragmentary. Here in my PhD thesis, using scanning electron microscopy, electrophysiology, behaviour, bioinformatics and molecular biology techniques, I have investigated tsetse flies (Glossina fuscipes fuscipes) olfaction using behaviourally well studied odorants, tsetse repellent by comparing with attractant odour. Insect olfaction is mediated by olfactory sensory neurons (OSNs), located in olfactory sensilla, which are cuticular structures exposed to the environment through pore and create a platform for chemical communication.
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Souleymane, Diallo. "Coding of tsetse repellents by olfactory sensory neurons: towards the improvement and the development of novel." University of the Western Cape, 2020. http://hdl.handle.net/11394/8236.

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Philosophiae Doctor - PhD
Tsetse flies are the biological vectors of human and animal trypanosomiasis and hence representant medical and veterinary importance. The sense of smell plays a significant role in tsetse and its ecological interaction, such as finding blood meal source, resting, and larvicidal sites and for mating. Tsetse olfactory behaviour can be exploited for their management; however, olfactory studies in tsetse flies are still fragmentary. Here in my PhD thesis, using scanning electron microscopy, electrophysiology, behaviour, bioinformatics and molecular biology techniques, I have investigated tsetse flies (Glossina fuscipes fuscipes) olfaction using behaviourally well studied odorants, tsetse repellent by comparing with attractant odour. Insect olfaction is mediated by olfactory sensory neurons (OSNs), located in olfactory sensilla, which are cuticular structures exposed to the environment through pore and create a platform for chemical communication. In the sensilla shaft the dendrite of OSNs are housed, which are protected by called the sensillum lymph produced by support cells and contains a variety of olfactory proteins, including the odorant binding protein (OBP) and chemosensory proteins (CSP). While on the dendrite of OSNs are expressed olfactory receptors. In my PhD, studies I tried to decipher the sense of smell in tsetse fly. In the second chapter, I demonstrated that G. f. fuscipes is equipped with diverse olfactory sensilla, that various from basiconic, trichoid and coeloconic. I also demonstrated, there is shape, length, number difference between sensilla types and sexual dimorphism. There is a major difference between male and female, while male has the unique basiconic sensilla, club shaped found in the pits, which is absent from female pits. In my third chapter, I investigated the odorant receptors which are expressed on the dendrite of the olfactory sensory neurons (OSNs). G. f. fuscipes has 42 ORs, which were not functionally characterised. I used behaviourally well studied odorants, tsetse repellents, composed of four components blend. I demonstrated that tsetse repellent is also a strong antifeedant for both G. pallidipes and G. f. fuscipes using feeding bioassays as compared to the attractant odour, adding the value of tsetse repellent. However, the attractant odour enhanced the feeding index. Using DREAM (deorphanization of receptors based on expression alterations of mRNA levels). I found that in G. f. fuscipes, following a short in vivo exposure to the individual tsetse repellent component as well as an attractant volatile chemical, OSNs that respond to these compounds altered their mRNA expression in two opposite direction, significant downregulation and upregulation in their number of transcripts corresponding to the OR that they expressed and interacted with odorant. Also, I found that the odorants with opposite valence already segregate distinctly at the cellular and molecular target at the periphery, which is the reception of odorants by OSNs, which is the basis of sophisticated olfactory behaviour. Deorphanization of ORs in none model insect is a challenge, here by combining DREAM with molecular dynamics, as docking score, physiology and homology modelling with Drosophila a well-studied model insects, I was able to predict putative receptors of the tsetse repellent components and an attractant odour. However, many ORs were neutral, showing they were not activated by the odorants, demonstrating the selectivity of the technique as well as the receptors. In my fourth chapter, I investigated the OBPs structures and their interaction with odorants molecules. I demonstrated that OBPs are expressed both in the antenna, as well as in other tissues, such as legs. I also demonstrated that there are variations in the expression of OBPs between tissues as well as sexes. I also demonstrated that odorants induced a fast alteration in OBP mRNA expression, some odorants induced a decrease in the transcription of genes corresponding to the activated OBP and others increased the expression by many fold in OBPs in live insect, others were neutral after 5 hours of exposure. Moreover, with subsequent behavioural data showed that the behavioural response of G. f. fuscipes toward 1-octen-3-ol decreased significantly when 1-octen-3-ol putative OBPs were silenced with feeding of double-stranded RNA (dsRNA). In summary, our finding whereby odorant exposure affects the OBPs mRNA, their physiochemical properties and the silencing of these OBPs affected the behavioural response demonstrate that the OBPs are involved in odour detection that affect the percept of the given odorant. The expression of OBPs in olfactory tissues, antenna and their interaction with odorant and their effect on behavioural response when silenced shows their direct involvement in odour detection and reception. Furthermore, their expression in other tissues such as legs indicates they might also have role in other physiological functions, such as taste.
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Paul, Uchenna Prince. "Fluorescence Detectors for Proteins and Toxic Heavy Metals." Diss., CLICK HERE for online access, 2004. http://contentdm.lib.byu.edu/ETD/image/etd416.pdf.

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Kurishita, Yasutaka. "Development of Molecular Tools for Analysis and Imaging of ATP and Other Biomolecules Based on Coordination Chemistry." 京都大学 (Kyoto University), 2014. http://hdl.handle.net/2433/188614.

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Fierro, Fabrizio Verfasser], Paolo [Akademischer Betreuer] Carloni, and Marc [Akademischer Betreuer] [Spehr. "Human chemosensory G-protein coupled receptors : insight into agonist binding from bioinformatics and multiscale simulations / Fabrizio Fierro ; Paolo Carloni, Marc Spehr." Aachen : Universitätsbibliothek der RWTH Aachen, 2019. http://d-nb.info/1193181550/34.

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Books on the topic "Chemosensory proteins"

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

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Pearce, Tim C. Chemosensation. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780199674923.003.0017.

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Olfaction in animals still surpasses any technological solution to chemical sensing yet conceived. While certain classes of molecular detection technologies may be capable of high sensitivity to a restricted number of compounds, unique to the biological system is its astonishing dynamic range (over 10 orders of magnitude), combining both extreme levels of sensitivity to certain key compounds of behavioural importance and varying levels of discrimination between an almost infinite variety of ligands, presented both individually and in complex combinations. For over 30 years the olfactory system of insects and mammals has provided biological sensing factors, rich inspiration, and processing principles for use in developing chemical sensing technologies. Here we focus on three such technological translations: recent rapid progress in measuring directly from olfactory binding/receptor proteins and chemosensory neurons as a biohybrid solution to chemical sensing; olfactory system based processing principles and architectures that have been applied to existing chemosensor technologies to achieve real-world sensing performance gains; and full-blown neuromorphic implementations of the olfactory pathways of animals.
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Book chapters on the topic "Chemosensory proteins"

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Zhu, Jiao, Immacolata Iovinella, Francesca Romana Dani, Paolo Pelosi, and Guirong Wang. "Chemosensory Proteins: A Versatile Binding Family." In Olfactory Concepts of Insect Control - Alternative to insecticides, 147–69. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-05165-5_6.

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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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Tsien, Roger Y. "New Fluorescent Readouts for Protein Interactions, Gene Expression, and Membrane Potential." In Chemosensors of Ion and Molecule Recognition, 17–21. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-3973-1_2.

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Marcinek, Patrick, Christiane Geithe, and Dietmar Krautwurst. "Chemosensory G Protein-Coupled Receptors (GPCR) in Blood Leukocytes." In Topics in Medicinal Chemistry, 151–73. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/7355_2016_101.

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Picimbon, Jean-François. "Evolution of Protein Physical Structures in Insect Chemosensory Systems." In Olfactory Concepts of Insect Control - Alternative to insecticides, 231–63. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-05165-5_10.

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Cieplak, Maciej, and Wlodzimierz Kutner. "CHAPTER 9. Protein Determination Using Molecularly Imprinted Polymer (MIP) Chemosensors." In Polymer Chemistry Series, 282–329. Cambridge: Royal Society of Chemistry, 2018. http://dx.doi.org/10.1039/9781788010474-00282.

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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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Leone, Serena, Alessandro Emendato, Roberta Spadaccini, and Delia Picone. "Solution structure of insect CSP and OBPs by NMR." In Odorant Binding and Chemosensory Proteins, 169–92. Elsevier, 2020. http://dx.doi.org/10.1016/bs.mie.2020.04.063.

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Steinbrecht, Rudolf Alexander. "Fine structure immunocytochemistry—An important tool for research on odorant-binding proteins." In Odorant Binding and Chemosensory Proteins, 259–78. Elsevier, 2020. http://dx.doi.org/10.1016/bs.mie.2020.04.064.

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Conference papers on the topic "Chemosensory proteins"

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"Development of a biosensor for rapid detection of insecticide based on insect-derived chemosensory proteins and graphene nanocellulose paper." In 2016 ASABE International Meeting. American Society of Agricultural and Biological Engineers, 2016. http://dx.doi.org/10.13031/aim.20162460030.

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Wang, Ran. "Candidate chemosensory protein genes in whiteflyBemisiatabaci by transcriptome analysis." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.114182.

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Liu, Chenxi. "Functional characterization of a chemosensory protein in a natural predator, Chrysopa pallens,indicates involvement of the protein in prey location." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.114100.

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