0000000000266698

AUTHOR

Christian Cambillau

showing 4 related works from this author

The Odorant-Binding Proteins of the Spider Mite Tetranychus urticae

2021

Spider mites are one of the major agricultural pests, feeding on a large variety of plants. As a contribution to understanding chemical communication in these arthropods, we have characterized a recently discovered class of odorant-binding proteins (OBPs) in Tetranychus urticae. As in other species of Chelicerata, the four OBPs of T. urticae contain six conserved cysteines paired in a pattern (C1–C6, C2–C3, C4–C5) differing from that of insect counterparts (C1–C3, C2–C5, C4–C6). Proteomic analysis uncovered a second family of OBPs, including twelve members that are likely to be unique to T. urticae. A three-dimensional model of TurtOBP1, built on the recent X-ray structure of Varroa destruc…

0106 biological sciences0301 basic medicineModels MolecularProteomicsProteomeOdorant bindingProtein ConformationInsectLigandsReceptors Odorant01 natural scienceschemistry.chemical_compoundTetranychus urticaeBiology (General)SpectroscopyPhylogenymedia_commonmass spectrometryGeneticsbiologyligand-bindingMolecular Structurespider mitesGeneral MedicineTetranychus urticaeComputer Science ApplicationsChemistryConiferyl aldehydedisulfide bridgesTetranychidaeProtein Bindingspider mites.QH301-705.5media_common.quotation_subjectodorant-binding proteinsCatalysisArticleInorganic Chemistry03 medical and health sciencesSpider mite<i>Tetranychus urticae</i>AnimalsAmino Acid SequencePhysical and Theoretical ChemistryQD1-999Molecular BiologySpiderOrganic Chemistrybiology.organism_classification010602 entomology030104 developmental biologychemistryVarroa destructorOdorantsChelicerataInternational Journal of Molecular Sciences
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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…

Models MolecularProtein FoldingProtein ConformationMolecular Sequence DataCockroachesCrystallography X-RayLigandsBiochemistryBombykolchemistry.chemical_compoundBombyx moribiology.animalAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyFluorescent DyesCockroachbiologySequence Homology Amino AcidCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationLigand (biochemistry)BombyxButanonesTransport proteinKineticschemistryBiochemistryHelixBiophysicsPheromoneInsect ProteinsFemalePheromone binding proteinCarrier ProteinsProtein BindingThe Journal of biological chemistry
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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…

Carrier Proteins/*genetics/*metabolismProtein familymedia_common.quotation_subjectMolecular Sequence DataCockroachesEndopterygotaInsectBiochemistryPolymerase Chain ReactionPheromonesbiology.animalPheromones/*metabolismAnimalsPheromone bindingAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceIn Situ Hybridizationmedia_commonCockroachbiologyBase SequenceMolecularCell Biologybiology.organism_classificationRecombinant ProteinsBiochemistryCockroaches/*physiologyInsect ProteinsPheromoneCarrier ProteinsPheromone binding proteinInsect Proteins/genetics/metabolismRecombinant Proteins/chemistry/metabolismResearch ArticleCloning
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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…

Molecular Sequence DataCockroachesCrystallography X-Raymedicine.disease_causelaw.inventionStructural Biologylawbiology.animalmedicineAnimalsAmino Acid SequenceCrystallizationEscherichia coliCockroachSequence Homology Amino AcidbiologyChemistryResolution (electron density)General MedicinePeriplasmic spaceRecombinant ProteinsCrystallographySex pheromoneRecombinant DNAInsect ProteinsFemaleCarrier ProteinsCrystallizationPheromone binding proteinSequence AlignmentActa Crystallographica Section D Biological Crystallography
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