Journal articles: 'Odorant Binding Proteins'

1

Pelosi, Paolo. "Odorant-Binding Proteins." Critical Reviews in Biochemistry and Molecular Biology 29, no. 3 (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 (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, et al. "Mammalian odorant binding proteins." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1482, no. 1-2 (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, et al. "Interactions Between Odorants and Glutathione Transferases in the Human Olfactory Cleft." Chemical Senses 45, no. 8 (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 (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 (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 (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 (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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STEINBRECHT, RUDOLF ALEXANDER. "Odorant-Binding Proteins: Expression and Function." Annals of the New York Academy of Sciences 855, no. 1 OLFACTION AND (1998): 323–32. http://dx.doi.org/10.1111/j.1749-6632.1998.tb10591.x.

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Krieger, J., H. Gänβle, K. Raming, and H. Breer. "Odorant binding proteins of Heliothis virescens." Insect Biochemistry and Molecular Biology 23, no. 4 (1993): 449–56. http://dx.doi.org/10.1016/0965-1748(93)90052-t.

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Pes, Daniela, and Paolo Pelosi. "Odorant-binding proteins of the mouse." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 112, no. 3 (1995): 471–79. http://dx.doi.org/10.1016/0305-0491(95)00063-1.

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Shirley, S. G., E. H. Polak, R. A. Mather, and G. H. Dodd. "The effect of concanavalin A on the rat electro-olfactogram. Differential inhibition of odorant response." Biochemical Journal 245, no. 1 (1987): 175–84. http://dx.doi.org/10.1042/bj2450175.

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When the rat olfactory mucosa is treated with concanavalin A, it subsequently shows diminished sensitivity towards 60% of the 112 odorants tested (as judged by the amplitude of the electro-olfactogram response). Odorants containing four to six carbon atoms tend to show the largest (absolute) diminutions, suggesting a receptor for this kind of odorant, although the structural specificity is weak. The receptor seems to be of particular importance in the detection of thiols, carboxylic acids and hydrocarbons of the above size, since these compounds loose the highest proportion of their original signal. The concanavalin A appears to be binding to the glycan of one or more cell-surface proteins. The binding may be at, or close to, at least one odorant receptor.

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Ha, Tal Soo, and Dean P. Smith. "Recent Insights into Insect Olfactory Receptors and Odorant-Binding Proteins." Insects 13, no. 10 (2022): 926. http://dx.doi.org/10.3390/insects13100926.

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Human and insect olfaction share many general features, but insects differ from mammalian systems in important ways. Mammalian olfactory neurons share the same overlying fluid layer in the nose, and neuronal tuning entirely depends upon receptor specificity. In insects, the olfactory neurons are anatomically segregated into sensilla, and small clusters of olfactory neurons dendrites share extracellular fluid that can be independently regulated in different sensilla. Small extracellular proteins called odorant-binding proteins are differentially secreted into this sensillum lymph fluid where they have been shown to confer sensitivity to specific odorants, and they can also affect the kinetics of the olfactory neuron responses. Insect olfactory receptors are not G-protein-coupled receptors, such as vertebrate olfactory receptors, but are ligand-gated ion channels opened by direct interactions with odorant molecules. Recently, several examples of insect olfactory neurons expressing multiple receptors have been identified, indicating that the mechanisms for neuronal tuning may be broader in insects than mammals. Finally, recent advances in genome editing are finding applications in many species, including agricultural pests and human disease vectors.

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Dear, T. Neil, Kathryn Campbell, and Terence H. Rabbitts. "Molecular cloning of putative odorant-binding and odorant-metabolizing proteins." Biochemistry 30, no. 43 (1991): 10376–82. http://dx.doi.org/10.1021/bi00107a003.

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Kim, Min-Su, Allen Repp, and Dean P. Smith. "LUSH Odorant-Binding Protein Mediates Chemosensory Responses to Alcohols in Drosophila melanogaster." Genetics 150, no. 2 (1998): 711–21. http://dx.doi.org/10.1093/genetics/150.2.711.

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Abstract The molecular mechanisms mediating chemosensory discrimination in insects are unknown. Using the enhancer trapping approach, we identified a new Drosophila mutant, lush, with odorant-specific defects in olfactory behavior. lush mutant flies are abnormally attracted to high concentrations of ethanol, propanol, and butanol but have normal chemosensory responses to other odorants. We show that wild-type flies have an active olfactory avoidance mechanism to prevent attraction to concentrated alcohol, and this response is defective in lush mutants. This suggests that the defective olfactory behavior associated with the lush mutation may result from a specific defect in chemoavoidance. lush mutants have a 3-kb deletion that produces a null allele of a new member of the invertebrate odorant-binding protein family, LUSH. LUSH is normally expressed exclusively in a subset of trichoid chemosensory sensilla located on the ventral-lateral surface of the third antennal segment. LUSH is secreted from nonneuronal support cells into the sensillum lymph that bathes the olfactory neurons within these sensilla. Reintroduction of a cloned wild-type copy of lush into the mutant background completely restores wild-type olfactory behavior, demonstrating that this odorant-binding protein is required in a subset of sensilla for normal chemosensory behavior to a subset of odorants. These findings provide direct evidence that odorant-binding proteins are required for normal chemosensory behavior in Drosophila and may partially determine the chemical specificity of olfactory neurons in vivo.

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18

Li, Keming, Shanning Wang, Kang Zhang, et al. "Odorant Binding Characteristics of Three Recombinant Odorant Binding Proteins in Microplitis mediator (Hymenoptera: Braconidae)." Journal of Chemical Ecology 40, no. 6 (2014): 541–48. http://dx.doi.org/10.1007/s10886-014-0458-5.

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Diallo, Souleymane, Mohd Shahbaaz, JohnMark O. Makwatta, et al. "Antennal Enriched Odorant Binding Proteins Are Required for Odor Communication in Glossina f. fuscipes." Biomolecules 11, no. 4 (2021): 541. http://dx.doi.org/10.3390/biom11040541.

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Olfaction is orchestrated at different stages and involves various proteins at each step. For example, odorant-binding proteins (OBPs) are soluble proteins found in sensillum lymph that might encounter odorants before reaching the odorant receptors. In tsetse flies, the function of OBPs in olfaction is less understood. Here, we investigated the role of OBPs in Glossina fuscipes fuscipes olfaction, the main vector of sleeping sickness, using multidisciplinary approaches. Our tissue expression study demonstrated that GffLush was conserved in legs and antenna in both sexes, whereas GffObp44 and GffObp69 were expressed in the legs but absent in the antenna. GffObp99 was absent in the female antenna but expressed in the male antenna. Short odorant exposure induced a fast alteration in the transcription of OBP genes. Furthermore, we successfully silenced a specific OBP expressed in the antenna via dsRNAi feeding to decipher its function. We found that silencing OBPs that interact with 1-octen-3-ol significantly abolished flies’ attraction to 1-octen-3-ol, a known attractant for tsetse fly. However, OBPs that demonstrated a weak interaction with 1-octen-3-ol did not affect the behavioral response, even though it was successfully silenced. Thus, OBPs’ selective interaction with ligands, their expression in the antenna and their significant impact on behavior when silenced demonstrated their direct involvement in olfaction.

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Gonçalves, Filipa, Artur Ribeiro, Carla Silva, and Artur Cavaco-Paulo. "Biotechnological applications of mammalian odorant-binding proteins." Critical Reviews in Biotechnology 41, no. 3 (2021): 441–55. http://dx.doi.org/10.1080/07388551.2020.1853672.

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Deyu, Zhang, and Walter Soares Leal. "Conformational Isomers of Insect Odorant-Binding Proteins." Archives of Biochemistry and Biophysics 397, no. 1 (2002): 99–105. http://dx.doi.org/10.1006/abbi.2001.2660.

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Price, Steven, and Amy Willey. "Effects of antibodies against odorant binding proteins on electrophysiological responses to odorants." Biochimica et Biophysica Acta (BBA) - General Subjects 965, no. 2-3 (1988): 127–29. http://dx.doi.org/10.1016/0304-4165(88)90047-5.

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Nakamura, Tadashi, Yoshihiro Noumi, Hiroyuki Yamakawa, et al. "Enhancement of the Olfactory Response by Lipocalin Cp-Lip1 in Newt Olfactory Receptor Cells: An Electrophysiological Study." Chemical Senses 44, no. 7 (2019): 523–33. http://dx.doi.org/10.1093/chemse/bjz048.

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Abstract Previously, we have detected the expression of 2 lipocalin genes (lp1 and lp2) in the olfactory epithelium of the Japanese newt Cynops pyrrhogaster. Recombinant proteins of these genes (Cp-Lip1 and Cp-Lip2, respectively) exhibited high affinities to various odorants, suggesting that they work like the odorant-binding proteins (OBPs). However, the physiological functions of OBP generally remain inconclusive. Here, we examined the effect of Cp-Lip1 on the electrophysiological responses of newt olfactory receptor cells. We observed that the electro-olfactogram induced by the vapor of an odorant with high affinity to Cp-Lip1 appeared to increase in amplitude when a tiny drop of Cp-Lip1 solution was dispersed over the olfactory epithelium. However, the analysis was difficult because of possible interference by intrinsic components in the nasal mucus. We subsequently adopted a mucus-free condition by using suction electrode recordings from isolated olfactory cells, in which impulses were generated by puffs of odorant solution. When various concentration (0–5 µM) of Cp-Lip1 was mixed with the stimulus solution of odorants highly affinitive to Cp-Lip1, the impulse frequency increased in a concentration-dependent manner. The increase by Cp-Lip1 was seen more evidently at lower concentration ranges of stimulus odorants. These results strongly suggest that Cp-Lip1 broadens the sensitivity of the olfactory cells toward the lower concentration of odorants, by which animals can detect very low concentration of odorants.

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Leal, Gabriel M., and Walter S. Leal. "Binding of a fluorescence reporter and a ligand to an odorant-binding protein of the yellow fever mosquito, Aedes aegypti." F1000Research 3 (December 12, 2014): 305. http://dx.doi.org/10.12688/f1000research.5879.1.

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Odorant-binding proteins (OBPs), also named pheromone-binding proteins when the odorant is a pheromone, are essential for insect olfaction. They solubilize odorants that reach the port of entry of the olfactory system, the pore tubules in antennae and other olfactory appendages. Then, OBPs transport these hydrophobic compounds through an aqueous sensillar lymph to receptors embedded on dendritic membranes of olfactory receptor neurons. Structures of OBPs from mosquito species have shed new light on the mechanism of transport, although there is considerable debate on how they deliver odorant to receptors. An OBP from the southern house mosquito, Culex quinquefasciatus, binds the hydrophobic moiety of a mosquito oviposition pheromone (MOP) on the edge of its binding cavity. Likewise, it has been demonstrated that the orthologous protein from the malaria mosquito binds the insect repellent DEET on a similar edge of its binding pocket. A high school research project was aimed at testing whether the orthologous protein from the yellow fever mosquito, AaegOBP1, binds DEET and other insect repellents, and MOP was used as a positive control. Binding assays using the fluorescence reporter N-phenyl-1-naphtylamine (NPN) were inconclusive. However, titration of NPN fluorescence emission in AaegOBP1 solution with MOP led to unexpected and intriguing results. Quenching was observed in the initial phase of titration, but addition of higher doses of MOP led to a stepwise increase in fluorescence emission coupled with a blue shift, which can be explained at least in part by formation of MOP micelles to house stray NPN molecules.

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Leal, Gabriel M., and Walter S. Leal. "Binding of a fluorescence reporter and a ligand to an odorant-binding protein of the yellow fever mosquito, Aedes aegypti." F1000Research 3 (January 9, 2015): 305. http://dx.doi.org/10.12688/f1000research.5879.2.

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Odorant-binding proteins (OBPs), also named pheromone-binding proteins when the odorant is a pheromone, are essential for insect olfaction. They solubilize odorants that reach the port of entry of the olfactory system, the pore tubules in antennae and other olfactory appendages. Then, OBPs transport these hydrophobic compounds through an aqueous sensillar lymph to receptors embedded on dendritic membranes of olfactory receptor neurons. Structures of OBPs from mosquito species have shed new light on the mechanism of transport, although there is considerable debate on how they deliver odorant to receptors. An OBP from the southern house mosquito, Culex quinquefasciatus, binds the hydrophobic moiety of a mosquito oviposition pheromone (MOP) on the edge of its binding cavity. Likewise, it has been demonstrated that the orthologous protein from the malaria mosquito binds the insect repellent DEET on a similar edge of its binding pocket. A high school research project was aimed at testing whether the orthologous protein from the yellow fever mosquito, AaegOBP1, binds DEET and other insect repellents, and MOP was used as a positive control. Binding assays using the fluorescence reporter N-phenyl-1-naphtylamine (NPN) were inconclusive. However, titration of NPN fluorescence emission in AaegOBP1 solution with MOP led to unexpected and intriguing results. Quenching was observed in the initial phase of titration, but addition of higher doses of MOP led to a stepwise increase in fluorescence emission coupled with a blue shift, which can be explained at least in part by formation of MOP micelles to house stray NPN molecules.

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Wang, Ping, Richard F. Lyman, Trudy F. C. Mackay, and Robert R. H. Anholt. "Natural Variation in Odorant Recognition Among Odorant-Binding Proteins in Drosophila melanogaster." Genetics 184, no. 3 (2009): 759–67. http://dx.doi.org/10.1534/genetics.109.113340.

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27

Vyas, Meenal, Kamala Jayanthi Pagadala Damodaram, and Gandham Krishnarao. "Antennal Transcriptome of the Fruit-Sucking Moth Eudocima materna: Identification of Olfactory Genes and Preliminary Evidence for RNA-Editing Events in Odorant Receptors." Genes 13, no. 7 (2022): 1207. http://dx.doi.org/10.3390/genes13071207.

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Unappealing shriveled fruits are a characteristic of one of the most elusive fruit pests. The perpetrator, Eudocima materna, attacks the fruit at a fully formed stage and, therefore, the antennal transcriptome for this insect was deduced to identify the molecular elicitors involved in the attraction to its host plants. A total of 260 olfactory genes, including 16 odorant-binding proteins (OBPs), four pheromone-binding proteins (PBPs), 40 antennal-binding proteins (ABPs), 178 odorant receptors (ORs), 17 chemosensory proteins (CSPs) and five sensory neuron membrane proteins (SNMPs) were identified. Phylogenetic analysis shows the divergence of E. materna proteins from closely related lepidopterans and provides insights on genes that have exclusively evolved in this insect. STRING network analysis revealed interactions of olfactory proteins among themselves and the proteins of other groups. Interestingly, online tools predicted RNA-editing events in the odorant receptor sequences, suggesting the possibility of multiple protein forms. Transcripts matching transposable element sequences were also detected in the dataset. Thus, the work reported here provides a valuable resource to design molecular methods for pest control.

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Pelosi, P. "Diversity of Odorant-binding Proteins and Chemosensory Proteins in Insects." Chemical Senses 30, Supplement 1 (2005): i291—i292. http://dx.doi.org/10.1093/chemse/bjh229.

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Venthur, Herbert, Ana Mutis, Jing-Jiang Zhou, and Andrés Quiroz. "Ligand binding and homology modelling of insect odorant-binding proteins." Physiological Entomology 39, no. 3 (2014): 183–98. http://dx.doi.org/10.1111/phen.12066.

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Lobel, Dietrich, Silvana Marchese, Jurgen Krieger, Paolo Pelosi, and Heinz Breer. "Subtypes of odorant-binding proteins. Heterologous expression and ligand binding." European Journal of Biochemistry 254, no. 2 (1998): 318–24. http://dx.doi.org/10.1046/j.1432-1327.1998.2540318.x.

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Garibotti, Marina, Ambretta Navarrini, Anna Maria Pisanelli, and Paolo Pelosi. "Three Odorant-binding Proteins from Rabbit Nasal Mucosa." Chemical Senses 22, no. 4 (1997): 383–90. http://dx.doi.org/10.1093/chemse/22.4.383.

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Manai, R., E. Scorsone, L. Rousseau, et al. "Grafting odorant binding proteins on diamond bio-MEMS." Biosensors and Bioelectronics 60 (October 2014): 311–17. http://dx.doi.org/10.1016/j.bios.2014.04.020.

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Pelosi, Paolo, Rosa Mastrogiacomo, Immacolata Iovinella, Elena Tuccori, and Krishna C. Persaud. "Structure and biotechnological applications of odorant-binding proteins." Applied Microbiology and Biotechnology 98, no. 1 (2013): 61–70. http://dx.doi.org/10.1007/s00253-013-5383-y.

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Bonazza, Caroline, and Klaus Bonazza. "Kinetics of Odorant Recognition with a Graphene-Based Olfactory Receptor Mimicry." Chemosensors 10, no. 6 (2022): 203. http://dx.doi.org/10.3390/chemosensors10060203.

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Malaria vector mosquito species rely on a handful of specific pheromones for mating; one of them, sulcatone (6-methyl-5-hepten-2-one), is also found in human exudation. Therefore, a complete understanding of the insect’s olfaction, and rapid real-time methods for odorant detection, are required. Here, we mimic the odorant recognition of the nerve cells of an insect’s antenna with a synthetic graphene-based bio-electro-interfacial odorant receptor. By this means, we obtain the kinetics of the genuine odorant recognition reaction and compare them to electro-antennogram data that represent the more complex scenario of a living insect. The odorant-binding proteins OBP 9A and 9B only associate with their ligands weakly, showing KDs of between 2.1 mM and 3 mM, while the binding kinetics of OBP proteins depend on the structural feature of a cystine knot and are modulated by the local milieu within a protein-aided enhancement zone.

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Ma, Yu, Yu Li, Zhi-Qiang Wei, et al. "Identification and Functional Characterization of General Odorant Binding Proteins in Orthaga achatina." Insects 14, no. 3 (2023): 216. http://dx.doi.org/10.3390/insects14030216.

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The olfactory system in insects are crucial for recognition of host plants and oviposition sites. General odorant binding proteins (GOBPs) are thought to be involved in detecting odorants released by host plants. Orthaga achatina (Lepidoptera: Pyralidae) is one of the most serious pests of camphor trees, Cinnamomum camphora (L.) Presl, an important urban tree species in southern China. In this study, we study the GOBPs of O. achatina. Firstly, two full-length GOBP genes (OachGOBP1 and OachGOBP2) were successfully cloned according to transcriptome sequencing results, and real-time quantitative PCR measurements showed that both GOBP genes were specifically expressed in the antennae of both sexes, proposing their important roles in olfaction. Then, both GOBP genes were heterologous expressed in Escherichia coli and fluorescence competitive binding assays were conducted. The results showed that OachGOBP1 could bind Farnesol (Ki = 9.49 μM) and Z11-16: OH (Ki = 1.57 μM). OachGOBP2 has a high binding affinity with two camphor plant volatiles (Farnesol, Ki = 7.33 μM; α-Phellandrene, Ki = 8.71 μM) and two sex pheromone components (Z11-16: OAc, Ki = 2.84 μM; Z11-16: OH, Ki = 3.30 μM). These results indicate that OachGOBP1 and OachGOBP2 differ in terms of odorants and other ligands. Furthermore, key amino acid residues that bind to plant volatiles were identified in GOBPs using 3-D structure modeling and ligand molecular docking, predicting the interactions between the GOBPs and the host plant volatiles.

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Rihani, Karen, Jean-François Ferveur, and Loïc Briand. "The 40-Year Mystery of Insect Odorant-Binding Proteins." Biomolecules 11, no. 4 (2021): 509. http://dx.doi.org/10.3390/biom11040509.

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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 mouthparts, pheromone glands, reproductive organs, digestive tract and venom glands, remain to be investigated. This review provides an updated panorama on the varied structural aspects, binding properties, tissue expression and functional roles of insect OBPs.

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Calvello, M., A. Brandazza, A. Navarrini, et al. "Expression of odorant-binding proteins and chemosensory proteins in some Hymenoptera." Insect Biochemistry and Molecular Biology 35, no. 4 (2005): 297–307. http://dx.doi.org/10.1016/j.ibmb.2005.01.002.

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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 (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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Mastrogiacomo, Rosa, Immacolata Iovinella, and Elio Napolitano. "New fluorescent probes for ligand-binding assays of odorant-binding proteins." Biochemical and Biophysical Research Communications 446, no. 1 (2014): 137–42. http://dx.doi.org/10.1016/j.bbrc.2014.02.067.

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Liu, Zhao, Diogo M. Vidal, Zainulabeuddin Syed, Yuko Ishida, and Walter S. Leal. "Pheromone Binding to General Odorant-binding Proteins from the Navel Orangeworm." Journal of Chemical Ecology 36, no. 7 (2010): 787–94. http://dx.doi.org/10.1007/s10886-010-9811-5.

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Yang, Ling, Xiaoli Tian, Lianyou Gui, Fulian Wang, and Guohui Zhang. "Key Amino Acid Residues Involved in Binding Interactions between Bactrocera minax Odorant-Binding Protein 3 (BminOBP3) and Undecanol." Insects 14, no. 9 (2023): 745. http://dx.doi.org/10.3390/insects14090745.

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Insect odorant-binding proteins (OBPs) are significant in binding and transporting odorants to specific receptors. Our previous study demonstrated that BminOBP3 exhibited a strong affinity with undecanol. However, the binding mechanism between them remains unknown. Here, using homology modeling and molecular docking, we found that the C-terminus (I116-P122), especially the hydrogenbonds formed by the last three amino acid residues (V120, F121, and P122) of the C-terminus, is essential for BminOBP3′s ligand binding. Mutant binding assays showed that the mutant T-OBP3 that lacks C-terminus (I116-P122) displayed a significant decrease in affinity to undecanol (Ki = 19.57 ± 0.45) compared with that of the wild-type protein BminOBP3 (Ki = 11.59 ± 0.51). In the mutant 3D2a that lacks F121 and P122 and the mutant V120A in which V120 was replaced by alanine, the bindings to undecanol were completely abolished. In conclusion, the C-terminus plays a crucial role in the binding interactions between BminOBP3 and undecanol. Based on the results, we discussed the ligand-binding process of BminOBP3.

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Riboni, Nicolò, Costanza Spadini, Clotilde S. Cabassi, et al. "OBP-functionalized/hybrid superparamagnetic nanoparticles for Candida albicans treatment." RSC Advances 11, no. 19 (2021): 11256–65. http://dx.doi.org/10.1039/d1ra01112j.

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Pelosi, Paolo, Jiao Zhu, and Wolfgang Knoll. "Odorant-Binding Proteins as Sensing Elements for Odour Monitoring." Sensors 18, no. 10 (2018): 3248. http://dx.doi.org/10.3390/s18103248.

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Odour perception has been the object of fast growing research interest in the last three decades. Parallel to the study of the corresponding biological systems, attempts are being made to model the olfactory system with electronic devices. Such projects range from the fabrication of individual sensors, tuned to specific chemicals of interest, to the design of multipurpose smell detectors using arrays of sensors assembled in a sort of artificial nose. Recently, proteins have attracted increasing interest as sensing elements. In particular, soluble olfaction proteins, including odorant-binding proteins (OBPs) of vertebrates and insects, chemosensory proteins (CSPs) and Niemann-Pick type C2 (NPC2) proteins possess interesting characteristics for their use in sensing devices for odours. In fact, thanks to their compact structure, their soluble nature and small size, they are extremely stable to high temperature, refractory to proteolysis and resistant to organic solvents. Moreover, thanks to the availability of many structures solved both as apo-proteins and in complexes with some ligands, it is feasible to design mutants by replacing residues in the binding sites with the aim of synthesising proteins with better selectivity and improved physical properties, as demonstrated in a number of cases.

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Manoharan, Malini, Kannan Sankar, Bernard Offmann, and Sowdhamini Ramanathan. "Association of Putative Members to Family of Mosquito Odorant Binding Proteins: Scoring Scheme Using Fuzzy Functional Templates and Cys Residue Positions." Bioinformatics and Biology Insights 7 (January 2013): BBI.S11096. http://dx.doi.org/10.4137/bbi.s11096.

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Proteins may be related to each other very specifically as homologous subfamilies. Proteins can also be related to diverse proteins at the super family level. It has become highly important to characterize the existing sequence databases by their signatures to facilitate the function annotation of newly added sequences. The algorithm described here uses a scheme for the classification of odorant binding proteins on the basis of functional residues and Cys-pairing. The cysteine-based scoring scheme not only helps in unambiguously identifying families like odorant binding proteins (OBPs), but also aids in their classification at the subfamily level with reliable accuracy. The algorithm was also applied to yet another cysteine-rich family, where similar accuracy was observed that ensures the application of the protocol to other families.

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Sims, Cassie, Michael A. Birkett, and David M. Withall. "Enantiomeric Discrimination in Insects: The Role of OBPs and ORs." Insects 13, no. 4 (2022): 368. http://dx.doi.org/10.3390/insects13040368.

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Olfaction is a complex recognition process that is critical for chemical communication in insects. Though some insect species are capable of discrimination between compounds that are structurally similar, little is understood about how this high level of discrimination arises. Some insects rely on discriminating between enantiomers of a compound, demonstrating an ability for highly selective recognition. The role of two major peripheral olfactory proteins in insect olfaction, i.e., odorant-binding proteins (OBPs) and odorant receptors (ORs) has been extensively studied. OBPs and ORs have variable discrimination capabilities, with some found to display highly specialized binding capability, whilst others exhibit promiscuous binding activity. A deeper understanding of how odorant-protein interactions induce a response in an insect relies on further analysis such as structural studies. In this review, we explore the potential role of OBPs and ORs in highly specific recognition, specifically enantiomeric discrimination. We summarize the state of research into OBP and OR function and focus on reported examples in the literature of clear enantiomeric discrimination by these proteins.

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Vandermoten, Sophie, Frédéric Francis, Eric Haubruge, and Walter S. Leal. "Conserved Odorant-Binding Proteins from Aphids and Eavesdropping Predators." PLoS ONE 6, no. 8 (2011): e23608. http://dx.doi.org/10.1371/journal.pone.0023608.

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Brito, Nathália F., Daniele S. Oliveira, Thaisa C. Santos, Monica F. Moreira, and Ana Claudia A. Melo. "Current and potential biotechnological applications of odorant-binding proteins." Applied Microbiology and Biotechnology 104, no. 20 (2020): 8631–48. http://dx.doi.org/10.1007/s00253-020-10860-0.

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Silva, Carla, Teresa Matamá, Nuno G. Azoia, Catarina Mansilha, Margarida Casal, and Artur Cavaco-Paulo. "Odorant binding proteins: a biotechnological tool for odour control." Applied Microbiology and Biotechnology 98, no. 8 (2013): 3629–38. http://dx.doi.org/10.1007/s00253-013-5243-9.

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Qiao, Huili, Xiaoli He, Danuta Schymura, et al. "Cooperative interactions between odorant-binding proteins of Anopheles gambiae." Cellular and Molecular Life Sciences 68, no. 10 (2010): 1799–813. http://dx.doi.org/10.1007/s00018-010-0539-8.

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Sun, X., F. F. Zeng, M. J. Yan, A. Zhang, Z. X. Lu, and M. Q. Wang. "Interactions of two odorant-binding proteins influence insect chemoreception." Insect Molecular Biology 25, no. 6 (2016): 712–23. http://dx.doi.org/10.1111/imb.12256.

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Journal articles on the topic 'Odorant Binding Proteins'

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