Ligand-Interaction Kinetics of the Pheromone- Binding Protein from the Gypsy Moth, L. dispar: Insights into the Mechanism of Binding and Release

Gong, Yue; Pace, Tamara C. S.; Castillo, Carlos; Bohne, Cornelia; O’Neill, Melanie A.; Plettner, Erika

doi:10.1016/j.chembiol.2009.01.005

Cited by 52 publications

(78 citation statements)

References 42 publications

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“…These findings may be due to the abnormal kinetics of these OBP-ligand mixtures. For some OBP-ligand interactions, 5 min may be insufficient time to establish an equilibrium (Gong et al 2009a). The mathematical treatment that was used to extract K i values assumed that: 1) the ligand and probe compete for one binding site and 2) the three partners (competing ligand, 1-NPN and PBP) reach equilibrium.…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization, Expression Pattern, and Ligand-Binding Property of Three Odorant Binding Protein Genes from Dendrolimus tabulaeformis

Zhang

Wang

et al. 2014

J Chem Ecol

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Odorant binding proteins (OBPs) play important roles in insect olfactory processes. The Chinese pine caterpillar moth, Dendrolimus tabulaeformis (Lepidoptera, Lasiocampidae) is a serious economic pest in China, and the pheromones of this species have been identified to monitor their presence. However, the molecular mechanisms by which D. tabulaeformis perceive pheromones and host volatiles remain unknown. In this study, we identified and characterized three new OBPs, including one pheromone binding protein (PBP1) and two general odor binding proteins (GOBPs), from antennal cDNA of D. tabulaeformis. The deduced amino acid sequences of DtabPBP1, DtabGOBP1, and DtabGOBP2 revealed mature proteins of 140, 147, and 140 amino acids, respectively. Each has six cysteine residues in conserved positions relative to other known OBPs. Amino-acid alignments indicated that the two GOBPs are more conserved (DtabGOBP1 is 52.9–67.4 % identical to orthologs from other Lepidoptera, and DtabGOBP2 is 55.2–81.8 % identical) than the PBP (32.5–46.0 %). Real-time PCR indicated tissue- and sex-specific expression patterns of the three genes. DtabPBP1 was mainly expressed in the antennae of males, whereas female antennae had only 1.09 % the expression in male antennae. Both DtabGOBP1 and DtabGOBP2 were more highly expressed in antennae than in other tissues, while DtabGOBP1 was more abundant in male antennae and DtabGOBP2 in female antennae. In addition, the binding specificities of the three proteins were investigated, and all three OBPs exhibited high binding affinities for the pheromone component (5Z,7E)-5,7-dodecadien-1-yl propionate (Z5,E7-12:OPr). This suggests a role in binding pheromone for GOBPs, as well as PBP1, in D. tabulaeformis.Electronic supplementary materialThe online version of this article (doi:10.1007/s10886-014-0412-6) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Molecular Characterization, Expression Pattern, and Ligand-Binding Property of Three Odorant Binding Protein Genes from Dendrolimus tabulaeformis

Zhang

Wang

et al. 2014

J Chem Ecol

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“…Independent models were proposed for the biological role of each OBP in chemosensation. A pheromone-binding protein (PBP) of the gypsy moth Lymantria dispar , PBP2, is thought to function as a scavenger [12], [13]. Another PBP in the silkworm moth Bombyx mori , PBP1, is considered as a transporter for the ligand, bombykol [14].…”

Section: Introductionmentioning

confidence: 99%

Functional Evolution of Duplicated Odorant-Binding Protein Genes, Obp57d and Obp57e, in Drosophila

et al. 2012

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Odorant-binding proteins (OBPs) are extracellular proteins found in insect chemosensilla, where they participate in the sensing of odors, tastes, and pheromones. Although a large number of OBP genes have been identified in insect genomes, their molecular functions and biological roles have been clarified in limited cases. Two OBP genes, Obp57d and Obp57e, were involved in the evolution of host-plant preference in Drosophila sechellia. Comparative analyses of the Obp57d/e genomic sequences from 27 closely related species suggested that the two genes arose by tandem gene duplication and functionally diverged from each other. In this study, the functional evolution of Obp57d and Obp57e was examined by in vitro binding assays using recombinant proteins synthesized in a bacterial system. Compared to the ancestral Dpse\OBP57de, Dmel\OBP57d was more specialized to tridecanoic acid while Dmel\OBP57e was generalized regarding their binding affinity, suggesting that the two OBP genes underwent subfunctionalization and neofunctionalization. A behavioral analysis using knockout flies supported that the biological role is different between OBP57d and OBP57e in vivo. Site-directed mutagenesis of the evolutionarily conserved amino acids revealed that these residues play an important role in protein folding. These findings provide a clue to understanding how the repertoire of OBP genes is maintained in a genome under natural selection.

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“…The dendritic membrane (8) houses the olfactory receptors (7) and the sensory neuron membrane protein (6). The figure is from Gong et al, 9 reproduced with kind permission of Chemistry & Biology, © 2009 Elsevier. added to the organic phase using a 10 µL glass syringe from a 50 mg mL -1 stock solution in distilled n-hexane.…”

Section: Determination Of Partition Coefficientsmentioning

confidence: 98%

“…Experimental studies of these interactions and their kinetics have recently been reported. 9 Further insight could be achieved through molecular modeling and molecular dynamics (MD) simulations. With recent advances in computer technology, MD has become an excellent companion and a viable alternative to often costly and difficult experiments.…”

Section: Introductionmentioning

confidence: 99%

Partition coefficients of disparlure at hydrophobic/aqueous interfaces: A comparative experimental and theoretical study

et al. 2011

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The gypsy moth, Lymantria dispar, uses pheromones, such as (+)-disparlure, for communication. These pheromones are detected by the sensitive antennae of the male moth and travel through their aqueous environment to the sensory neuron, possibly with assistance from pheromone binding proteins (PBPs). The hydrophobicity of disparlure, which is of primary importance for its interactions with PBPs, can be measured by its partition coefficients. These coefficients for heptane/water and chloroform/water interfaces were obtained in this work experimentally and using molecular dynamics (MD) simulations. The agreement between the experimental and calculated values validates the choice of the force field parameters, which can thus be used in future MD simulations of the PBP-pheromone interactions.Résumé : La lymantride spongieuse, mite gitane, Lymantria dispar, fait appel à des phéromones, tel le (+)-disparlure, pour ses communications. Ces phéromones sont détectées par des antennes sensibles des lymantrides mâles et elles circulent dans leur environnement aqueux vers le neurone sensoriel, peut-être avec l'aide de protéines fixatrices de phéromones (PFP). Le caractère hydrophobe du disparlure qui est d'importance capitale pour ses interactions avec les PFP peut être mesuré par ses coefficients de partition. Dans ce travail, on a mesuré expérimentalement ces coefficients pour les systèmes heptane/eau et chloroforme/eau et on les a aussi calculés par la méthode de la dynamique moléculaire (DM). L'accord entre les valeurs calculées et celles obtenues expérimentalement valide le choix des paramètres de champ de force qui pourront être utilisés dans des simulations ultérieures de DM des interactions PFP/phéromone.Mots-clés : lymantride spongieuse, disparlure, coefficients de partition, caractère hydrophobe, époxyde, paramètres des potentiels optimisés pour des simulations de liquides, simulations de dynamiques moléculaires.[Traduit par la Rédaction]

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Ligand-Interaction Kinetics of the Pheromone- Binding Protein from the Gypsy Moth, L. dispar: Insights into the Mechanism of Binding and Release

Cited by 52 publications

References 42 publications

Molecular Characterization, Expression Pattern, and Ligand-Binding Property of Three Odorant Binding Protein Genes from Dendrolimus tabulaeformis

Molecular Characterization, Expression Pattern, and Ligand-Binding Property of Three Odorant Binding Protein Genes from Dendrolimus tabulaeformis

Functional Evolution of Duplicated Odorant-Binding Protein Genes, Obp57d and Obp57e, in Drosophila

Partition coefficients of disparlure at hydrophobic/aqueous interfaces: A comparative experimental and theoretical study

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