Search results for "Plant lipid transfer proteins"

showing 10 items of 16 documents

From elicitins to lipid-transfer proteins: a new insight in cell signalling involved in plant defence mechanisms.

2002

Elicitins and lipid-transfer proteins are small cysteine-rich lipid-binding proteins secreted by oomycetes and plant cells, respectively, that share some structural and functional properties. In spite of intensive work on their structure and diversity at the protein and genetic levels, the precise biological roles of lipid-transfer proteins remains unclear, although the most recent data suggest a role in somatic embryogenesis, in the formation of protective surface layers and in defence against pathogens. By contrast, elicitins are known elicitors of plant defence, and recent work demonstrating that elicitins and lipid-transfer proteins share the same biological receptors gives a new perspe…

0106 biological sciencesSomatic embryogenesisProtein ConformationDefence mechanismsPlant ScienceBiology01 natural sciencesFungal Proteins03 medical and health sciencesErgosterolReceptor030304 developmental biologyPlant DiseasesPlant Proteins0303 health sciencesBinding proteinAlgal ProteinsLysophosphatidylcholinesProteinsElicitinAntigens PlantLipidsImmunity InnateBiochemistryOomycetesProtein-lipid complexStress MechanicalSignal transductionCarrier ProteinsPlant lipid transfer proteins010606 plant biology & botanySignal TransductionTrends in plant science
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Crustacean Hemolymph Lipoproteins

2020

Lipoproteins mediate the transport of apolar lipids in the hydrophilic environment of physiological fluids such as the vertebrate blood and the arthropod hemolymph. In this overview, we will focus on the hemolymph lipoproteins in Crustacea that have received most attention during the last years: the high density lipoprotein/β-glucan binding proteins (HDL-BGBPs), the vitellogenins (VGs), the clotting proteins (CPs) and the more recently discovered large discoidal lipoproteins (dLPs). VGs are female specific lipoproteins which supply both proteins and lipids as storage material for the oocyte for later use by the developing embryo. Unusual within the invertebrates, the crustacean yolk protein…

0303 health sciencesanimal structuresfood.ingredientbiologyApolipoprotein Bfungi030302 biochemistry & molecular biology03 medical and health scienceschemistry.chemical_compoundVitellogeninHigh-density lipoproteinfoodBiochemistrychemistryYolkHemolymphbiology.proteinlipids (amino acids peptides and proteins)VitellogeninsPlant lipid transfer proteins030304 developmental biologyLipoprotein
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Identification of a Lipid Transfer Protein as a New Allergen From Morus alba Pollen.

2017

AdultMale010504 meteorology & atmospheric sciencesImmunologymedicine.disease_cause01 natural sciences03 medical and health sciencesYoung Adult0302 clinical medicineAllergenPollenBotanymedicineImmunology and AllergyHumans0105 earth and related environmental sciencesPlant Proteinsbiologybusiness.industryRhinitis Allergic SeasonalAllergensAntigens PlantMiddle Aged030228 respiratory systemProfilinbiology.proteinPollenIdentification (biology)Electrophoresis Polyacrylamide GelFemaleMorusbusinessCarrier ProteinsPlant lipid transfer proteinsJournal of investigational allergologyclinical immunology
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Analysis of protein composition of red wine in comparison with rosé and white wines by electrophoresis and high-pressure liquid chromatography-mass s…

2009

Wine proteins not only influence wine stability but are also being discussed as potential allergens. Proteins from red, rose, and white wines were enriched by dialysis and lyophilization followed by separation by SDS-PAGE. Significant differences were detected in the protein compositions of the analyzed wine varieties, and the major protein bands were identified by mass spectrometry after in-gel digestion with trypsin. In German Portugieser red wine, a total of 121 tryptic peptides were identified, which were attributed to 12 grape proteins and 6 proteins derived from yeast. Among the identified constituents are several proteins considered to influence wine stability and previously describe…

ElectrophoresisWineMass spectrometryHigh-performance liquid chromatographyMass SpectrometryFungal ProteinsTrypsinVitisChromatography High Pressure LiquidPlant ProteinsWineChromatographyMolecular massChemistrydigestive oral and skin physiologyfood and beveragesProteinsFast protein liquid chromatographyGeneral ChemistryAllergensAntigens PlantYeastWhite WineFruitGeneral Agricultural and Biological SciencesCarrier ProteinsPlant lipid transfer proteinsFood HypersensitivityJournal of agricultural and food chemistry
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Innate immune response triggered by triacyl lipid A is dependent on phospholipid transfer protein (PLTP) gene expression

2010

Hexaacyl lipopolysaccharide (LPS) aggregates in aqueous media, but its partially deacylated lipid A moiety forms monomers with weaker toxicity. Because plasma phospholipid transfer protein (PLTP) transfers hexaacyl LPS, its impact on metabolism and biological activity of triacyl lipid A in mice was addressed. Triacyl lipid A bound readily to plasma high-density lipoproteins (HDLs) when active PLTP was expressed [HDL-associated lipid A after 4.5 h: 59.1+/-16.0% of total in wild-type (WT) vs. 32.5+/-10.3% in PLTP-deficient mice, P0.05]. In the opposite to hexaacyl LPS, plasma residence time of lipid A was extended by PLTP, and proinflammatory cytokines were produced in higher amounts in WT th…

LipopolysaccharideMelanoma ExperimentalBiologyBiochemistryLipid AInterferon-gammaMicechemistry.chemical_compoundCell Line TumorPhospholipid transfer proteinGene expressionGeneticsAnimalsPhospholipid Transfer ProteinsMolecular BiologyCells CulturedChemokine CCL2Interleukin-6Tumor Necrosis Factor-alphaBiological activityMetabolismFlow CytometryMolecular biologyImmunity InnateMice Mutant StrainsInterleukin-10Lipid AGene Expression RegulationchemistryBiochemistryCytokineslipids (amino acids peptides and proteins)Plant lipid transfer proteinsBiotechnologyLipoproteinThe FASEB Journal
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The major allergen of the Parietaria pollen contains an LPS-binding region with immuno-modulatory activity

2013

Background The major allergens in Parietaria pollen, Par j 1 and Par j 2, have been identified as lipid transfer proteins. The family of the Par j 1 allergens is composed of two isoforms, which differ by the presence of a 37 amino acid peptide (Par37) exclusive to the Par j 1.0101 isoform. The goal of this study was to elucidate the biological properties of the Par37 peptide. Methods In silico analysis, spectrofluorimetric experiments and in vitro cell culture assays were used to identify the biological properties of Par37. In addition, a mouse model of sensitization was used to study the influence of Par37 in the murine immune response. Results In silico analysis predicted that Par37 displ…

LipopolysaccharidesGene isoformParietariaIn silicoMolecular Sequence DataImmunologySettore BIO/11 - Biologia MolecolarePeptideBiologyAntibodiesInterferon-gammaMiceIn vivoAnimalsHumansImmunologic FactorsImmunology and AllergyAmino Acid SequencePlant ProteinsPolymyxin Bchemistry.chemical_classificationanimal modelallergens; animal models; environment; pollens.Allergensbiology.organism_classificationIn vitroAmino acidParietariachemistryBiochemistryLeukocytes MononuclearCytokinesPollenpollens.FemalePeptidesenvironmentSequence AlignmentPlant lipid transfer proteinsSpleenallergenProtein Binding
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Specific adduction of plant lipid transfer protein by an allene oxide generated by 9-lipoxygenase and allene oxide synthase

2006

International audience; Lipid transfer proteins (LTPs) are ubiquitous plant lipid-binding proteins that have been associated with multiple developmental and stress responses. Although LTPs typically bind fatty acids and fatty acid derivatives in a non-covalent way, studies on the LTPs of barley seeds have identified an abundantly occurring covalently modified form, LTP1b, the lipid ligand of which has resisted clarification. In the present study, this adduct was identified as the {alpha}-ketol 9-hydroxy-10-oxo-12(Z)-octadecenoic acid. Further studies on the formation of LTP1b demonstrated that the ligand was introduced by nucleophilic attack of the free carboxylate group of the Asp-7 residu…

Models Molecular0106 biological sciencesMagnetic Resonance SpectroscopyTime FactorsLIPID TRANSFER PROTEINAlleneLipoxygenaseLigands01 natural sciencesBiochemistrySubstrate SpecificityMiceLipoxygenasechemistry.chemical_compoundJasmonate2. Zero hungerchemistry.chemical_classificationALLENE OXIDE SYNTHASEMice Inbred BALB C0303 health sciencesbiologyfood and beveragesLIPID TRANSFER PROTEIN;LTP;ALLENE OXIDE SYNTHASE;PROTEINE DE TRANSFERT DE LIPIDE;REPONSE DE LA PLANTEIntramolecular OxidoreductasessynthaseBiochemistryprotéineLTPPlant lipid transfer proteinsLinoleic acidGas Chromatography-Mass Spectrometry03 medical and health sciencesprotéine végétaleréaction de défenseBiosynthesisAnimals[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular Biologymécanisme de défense030304 developmental biologyHybridomasFatty acidHordeumCell BiologyOxylipinenzymeoxylipineModels Chemicalchemistrybiology.proteinREPONSE DE LA PLANTEPROTEINE DE TRANSFERT DE LIPIDECarrier Proteins010606 plant biology & botany
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A lipid transfer protein binds to a receptor involved in the control of plant defence responses

2001

AbstractLipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.

Models Molecular0106 biological sciencesTime FactorsProtein ConformationPlasma protein bindingLigands01 natural sciencesBiochemistryProtein structureStructural BiologyReceptorAllosteryTriticumComputingMilieux_MISCELLANEOUSPlant Proteins0303 health sciencesFungal proteinfood and beveragesCell biologyBiochemistryPlant lipid transfer proteinsAllosteric SiteProtein BindingReceptorPhytophthoraLipid transfer proteinAllosteric regulationBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding CompetitiveFungal Proteins03 medical and health sciencesTobaccoGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesDose-Response Relationship DrugAlgal ProteinsCell MembraneElicitinCell BiologyAntigens PlantModels TheoreticalLipid MetabolismElicitinCarrier Proteins010606 plant biology & botanyFEBS Letters
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Multiple IgE recognition on the major allergen of the Parietaria pollen Par j 2

2015

The interaction between IgE antibodies and allergens is a key event in triggering an allergic reaction. The characterization of this region provides information of paramount importance for diagnosis and therapy. Par j 2 Lipid Transfer Protein is one of the most important allergens in southern Europe and a well-established marker of sensitization in Parietaria pollen allergy. The main aim of this study was to map the IgE binding regions of this allergen and to study the pattern of reactivity of individual Parietaria-allergic patients. By means of gene fragmentation, six overlapping peptides were expressed in Escherichia coli, and their IgE binding activity was evaluated by immunoblotting in …

Models MolecularParietariaAdolescentBlotting WesternImmunoblottingMolecular Sequence DataEpitope mappingImmunologyProtein domainImmunoglobulin Emedicine.disease_causeEpitopelaw.inventionEpitopesAllergenlawmedicineHumansComputer SimulationAmino Acid SequenceCloning MolecularChildParietaria IgE Epitope mapping Molecular biology.Molecular BiologybiologyRhinitis Allergic SeasonalAllergensImmunoglobulin Ebiology.organism_classificationRecombinant ProteinsParietariaEpitope mappingImmunologybiology.proteinRecombinant DNAPollenElectrophoresis Polyacrylamide GelIgEPlant lipid transfer proteinsMolecular Immunology
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Fatty acids bind to the fungal elicitor cryptogein and compete with sterols

2001

Abstract Cryptogein is a proteinaceous elicitor of plant defense reactions which also exhibits sterol carrier properties. In this study, we report that this protein binds fatty acids. The stoichiometry of the fatty acid–cryptogein complex is 1:1. Linoleic acid and dehydroergosterol compete for the same site, but elicitin affinity is 27 times lower for fatty acid than for sterol. We show that C7 to C12 saturated and C16 to C22 unsaturated fatty acids are the best ligands. The presence of double bonds markedly increases the affinity of cryptogein for fatty acids. A comparison between elicitins and known lipid transfer proteins is discussed.

Phytophthora0106 biological sciencesDouble bondLinoleic acidBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding Competitive01 natural sciencesBiochemistryFungal ProteinsLinoleic AcidLIAISON MOLECULAIREStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundStructural BiologyErgosterolGeneticsPlant defense against herbivoryMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSSterol030304 developmental biologychemistry.chemical_classification0303 health sciencesAlgal ProteinsFatty AcidsProteinsFatty acidLipid–protein interactionElicitinCell BiologyFatty acidElicitinSterol3. Good healthElicitorSterolschemistryBiochemistrylipids (amino acids peptides and proteins)Plant lipid transfer proteinsProtein Binding010606 plant biology & botany
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