0000000000266695

AUTHOR

Jiao Zhu

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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Lipocalins in Arthropod Chemical Communication.

2021

Abstract Lipocalins represent one of the most successful superfamilies of proteins. Most of them are extracellular carriers for hydrophobic ligands across aqueous media, but other functions have been reported. They are present in most living organisms including bacteria. In animals they have been identified in mammals, molluscs, and arthropods; sequences have also been reported for plants. A subgroup of lipocalins, referred to as odorant-binding proteins (OBPs), mediate chemical communication in mammals by ferrying specific pheromones to the vomeronasal organ. So far, these proteins have not been reported as carriers of semiochemicals in other living organisms; instead chemical communicatio…

arthropods; chemical communication; insects; lipocalins; odorant-binding proteins; phylogenesisArthropod AntennaeAcademicSubjects/SCI01140Vomeronasal organProtein familyGenome Insectodorant-binding proteinsphylogenesisLipocalinBiologyarthropodsPheromones03 medical and health sciences0302 clinical medicineGene duplicationGeneticsAnimalsinsectsGeneEcology Evolution Behavior and Systematics030304 developmental biology0303 health sciencesintegumentary systemAcademicSubjects/SCI01130chemical communicationbiology.organism_classificationLipocalinsAnimal CommunicationEvolutionary biologyPhylogenesisSex pheromoneArthropod030217 neurology & neurosurgeryResearch ArticleGenome biology and evolution
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Ligand-binding assays with OBPs and CSPs

2020

Assessing the ligand-binding properties of OBPs and CSPs is essential for understanding their physiological function. It also provides basic information when these proteins are used as biosensing elements for instrumental measurement of odors. Although different approaches have been applied in the past to evaluate the affinity of receptors and soluble binding proteins to their ligands, using a fluorescent reporter represents the method of choice for OBPs and CSPs. It offers the advantages of working at the equilibrium, being simple, fast and inexpensive, without requiring the use of radioactive tracers. However, as an indirect method, the fluorescence competitive binding approach presents d…

Physiological functionFluorescent reporterChemistryCompetitive bindingLigand binding assayComputational biology1-aminoanthracene
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Site-directed mutagenesis of odorant-binding proteins

2020

Modifying the affinity of odorant-binding proteins (OBPs) to small ligands by replacement of specific residues in the binding pocket may lead to several technological applications. Thanks to their compact and stable structures, OBPs are currently regarded as the best candidates to be used in biosensing elements for odorants and volatiles detection. The wide and rich information on the structure of these proteins both in their apo-forms and in complexes with specific ligands provides guidelines to design reliable mutants to monitor specific targets. The same engineered proteins may also find applications in the slow release of pheromones and other chemicals in the environment, as well as in …

ChemistryOdorant bindingBinding pocketMutagenesis (molecular biology technique)Computational biologyAmino acid residueSite-directed mutagenesis
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