Search results for "Pheromone binding"
showing 7 items of 7 documents
Coupling transcriptomics and behaviour to unveil the olfactory system of Spodoptera exigua larvae
2020
AbstractChemoreception in insects is crucial for many aspects related to food seeking, enemy avoidance, and reproduction. Different families of receptors and binding proteins interact with chemical stimuli, including odorant receptors (ORs), ionotropic receptors (IRs), gustatory receptors (GRs), odorant binding proteins (OBPs) and chemosensory proteins (CSPs). In this work, we describe the chemosensory-related gene repertoire of the worldwide spread pest Spodoptera exigua (Lepidoptera: Noctuide) focusing on the transcripts expressed in larvae, which feed on many horticultural crops producing yield losses. A comprehensive de novo assembly that includes reads from chemosensory organs of larva…
A pheromone-binding protein from the cockroach Leucophaea maderae: cloning, expression and pheromone binding
2003
0264-6021 (Print) Journal Article; Odorant-binding proteins (OBPs) are thought to transport volatile compounds from air to their receptors through the sensillary lymph. In this protein family, the subgroup of pheromone-binding proteins (PBPs) is specifically tuned to the perception of the sexual pheromone. To date, the description of OBPs has been restricted to Endopterygota and Paraneoptera. Their expression in Orthopteroid has been hypothesized, but no evidence of OBP has been produced in this assemblage to date. In the present study, we describe the first OBP from a Dictyopteran insect that belongs to the cockroach Leucophaea maderae. The PBP of L. maderae (PBPLma) shares all the hallmar…
Conformational Change in the Pheromone-binding Protein fromBombyx mori Induced by pH and by Interaction with Membranes
1999
The pheromone-binding protein (PBP) from Bombyx mori was expressed in Escherichia coli periplasm. It specifically bound radiolabeled bombykol, the natural pheromone for this species. It appeared as a single band both in native and SDS-polyacrylamide gel electrophoresis and was also homogeneous in most chromatographic systems. However, in ion-exchange chromatography, multiple forms sometimes appeared. Attempts to separate them revealed that they could be converted into one another. Analysis of the protein by circular dichroism and fluorescence spectroscopy demonstrated that its tertiary structure was sensitive to pH changes and that a dramatic conformational transition occurred between pH 6.…
The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism.
2003
Pheromone-binding proteins (PBPs) are small helical proteins found in sensorial organs, particularly in the antennae, of moth and other insect species. They were proposed to solubilize and carry the hydrophobic pheromonal compounds through the antennal lymph to receptors, participating thus in the peri-receptor events of signal transduction. The x-ray structure of Bombyx mori PBP (BmorPBP), from male antennae, revealed a six-helix fold forming a cavity that contains the pheromone bombykol. We have identified a PBP (LmaPBP) from the cockroach Leucophaea maderae in the antennae of the females, the gender attracted by pheromones in this species. Here we report the crystal structure of LmaPBP a…
Crystallization and preliminary crystallographic study of a pheromone-binding protein from the cockroachLeucophaea maderae
2002
Pheromone-binding proteins (PBPs) are small helical proteins (13-18 kDa) present in various sensory organs of moths and other insect species. An antennal protein from the cockroach Leucophaea maderae (LmaPBP) has been found to share all the hallmarks of the PBP family and is expressed specifically in the female adult antennae, the gender that perceives the sex pheromone. Here, the crystallization of LmaPBP expressed as a recombinant protein in Escherichia coli periplasm is reported. Crystals of LmaPBP were obtained by the sitting-drop vapour-diffusion method using a nanodrop-dispensing robot. The protein crystallizes in two different crystal forms. Form 1 belongs to space group P1, with uni…
Attracted or repelled?--a matter of two neurons, one pheromone binding protein, and a chiral center.
1998
Abstract Two species of scarab beetles, the Osaka beetle (Anomala osakana) and the Japanese beetle (Popillia japonica), utilize the opposite enantiomers of japonilure, (Z)-5-(1-decenyl)oxacyclopentan-2-one, as their sex pheromones. Each species produces only one of the enantiomers that functions as its own sex pheromone and as a very strong behavioral antagonist for the other species. Using an integrated approach we tested whether the discrimination of these two opposite signals is due to selective filtering by pheromone binding proteins or whether it originates in the specificity of ligand–receptor interactions. We found that the antennae of each of these two scarab species contain only a …
Pheromone-binding proteins of scarab beetles.
1998
: We have characterized Pheromone binding proteins (PBPs) present in the antennae of several species of scarab beetles. In most cases there was only one class of PBP, which was expressed in both sexes. Both Anomala osakana and Popillia japonica possess a single PBP, highly homologous to each other. In each species the same PBP seems to recognize both enantiomers of japonilure, which have opposite biological functions, i.e., the sex Pheromone and the behavioral antagonist (stop signal). The purified PBP of A. osakana binds both enantiomers apparently with the same low affinity. Unexpectedly, these ligands were bound by moth PBPs, which utilize Pheromones with unrelated structures. These find…