Search results for "epitope(s)"

showing 10 items of 254 documents

Agonist and antagonist-dependent internalization of the human vasopressin V2 receptor.

1998

Abstract In this report we demonstrate that in HEK293 cells stably expressing the human V2vasopressin receptor, ligand-induced internalization of the hormone receptor occurs via the clathrin-dependent pathway. Studies of receptor trafficking either by direct visualization of the V2receptor by confocal microscopy or binding experiments show a rapid internalization (half-time 6–7 min). Blocking of the clathrin-dependent pathway by hypertonic sucrose increased vasopressin-induced cellular cAMP production and decreased the desensitization of the V2receptor–adenylyl cyclase system. Thus, internalization appears to be a major regulatory mechanism terminating vasopressin action in HEK293 cells. Tw…

VasopressinReceptors VasopressinTime Factorsmedia_common.quotation_subjectRecombinant Fusion ProteinseducationBiologyKidneyLigandsTransfectionlaw.inventionCell LineEpitopesDesensitization (telecommunications)Confocal microscopylawEnzyme-linked receptorHumansInternalizationReceptormedia_commonAntagonistCell BiologyClathrinPeptide FragmentsCell biologyHormone receptorAntidiuretic Hormone Receptor AntagonistsExperimental cell research
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The Efficacy of Antigen Processing Is Critical for Protection against Cytomegalovirus Disease in the Presence of Viral Immune Evasion Proteins▿

2009

ABSTRACT Cytomegaloviruses (CMVs) code for immunoevasins, glycoproteins that are specifically dedicated to interfere with the presentation of antigenic peptides to CD8 T cells. Nonetheless, the biological outcome is not an immune evasion of the virus, since CD8 T cells can control CMV infection even when immunoevasins are expressed. Here, we compare the processing of a protective and a nonprotective epitope derived from the same viral protein, the antiapoptotic protein M45 in the murine model. The data provide evidence to conclude that protection against CMVs critically depends on antigenic peptides generated in an amount sufficient to exhaust the inhibitory capacity of immunoevasins.

Viral proteinImmunologyAntigen presentationCytomegalovirusBiologyCD8-Positive T-Lymphocytesmedicine.disease_causeMicrobiologyVirusEpitopeEpitopesMiceViral ProteinsImmune systemAntigenVirologyRibonucleotide ReductasesmedicineCytotoxic T cellAnimalsHumansAntigen PresentationAntigen processingVirologyPeptide FragmentsInsect ScienceImmunologyCytomegalovirus InfectionsPathogenesis and ImmunityApoptosis Regulatory Proteins
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Immunogenic hotspots in the spacer domain of ADAMTS13 in immune‐mediated thrombotic thrombocytopenic purpura

2021

International audience; Background Immune-mediated thrombotic thrombocytopenic purpura (iTTP) is caused by anti-ADAMTS13 autoantibodies inducing a severe deficiency of ADAMTS13. Epitope mapping studies on samples obtained during acute iTTP episodes have shown that the iTTP immune response is polyclonal, with almost all patients having autoantibodies targeting the spacer domain of ADAMTS13.Objectives To identify the immunogenic hotspots in the spacer domain of ADAMTS13.Patients/methods A library of 11 full-length ADAMTS13 spacer hybrids was created in which amino acid regions of the spacer domain of ADAMTS13 were exchanged by the corresponding region of the spacer domain of ADAMTS1. Next, th…

autoantibodiesADAMTS13 Protein030204 cardiovascular system & hematologyEpitope03 medical and health sciencesEpitopes0302 clinical medicineVon Willebrand factorimmunophenotypinghemic and lymphatic diseasesHumansthrombotic thrombocytopenic purpurachemistry.chemical_classificationbiologyPurpura Thrombotic ThrombocytopenicAutoantibodyHematologyMolecular biologyADAMTS13ADAMTS133. Good healthAmino acidepitope mappingEpitope mappingchemistryPolyclonal antibodiesImmunoglobulin Gbiology.proteinDNA IntergenicAntibody[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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Identification of glucan-mannoprotein complexes in the cell wall of Candida albicans using a monoclonal antibody that reacts with a (1,6)- -glucan ep…

1995

The use of a novel monoclonal antibody (mAb) that reacts with (1,6)-beta-glucan has permitted the study of the different covalent linkages between glucan and mannoproteins in the cell wall of Candida albicans. The mAb JRR1 was originally raised by immunization with Zymolyase extracts from C. albicans cell walls, but it soon became apparent that it reacted with a (1,6)-beta-glucan epitope. By using this antibody, we show the existence of glucan-mannoprotein complexes between the (1,6)-beta-glucan epitope recognized by the antibody and cell wall mannoproteins. The topology of the (1,6)-beta-glucan in the cell wall of C. albicans has also been studied.

beta-Glucansmedicine.drug_classFluorescent Antibody Techniquemacromolecular substancesMonoclonal antibodyBinding CompetitiveMicrobiologyChromatography AffinityEpitopeMicrobiologyFungal ProteinsMannansCell wallEpitopesAntigenCell WallPolysaccharidesCandida albicansmedicineCandida albicansGlucansGlucanchemistry.chemical_classificationMembrane GlycoproteinsbiologyTunicamycinAntibodies Monoclonalbiology.organism_classificationCorpus albicanscarbohydrates (lipids)stomatognathic diseaseschemistrybiology.proteinAntibodyMicrobiology
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Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis.

2008

Abstract Background The interconversion of two important energy metabolites, 3-hydroxybutyrate and acetoacetate (the major ketone bodies), is catalyzed by D-3-hydroxybutyrate dehydrogenase (BDH1: EC 1.1.1.30), a NAD+-dependent enzyme. The eukaryotic enzyme is bound to the mitochondrial inner membrane and harbors a unique lecithin-dependent activity. Here, we report an advanced purification method of the mammalian BDH applied to the liver enzyme from jerboa (Jaculus orientalis), a hibernating rodent adapted to extreme diet and environmental conditions. Results Purifying BDH from jerboa liver overcomes its low specific activity in mitochondria for further biochemical characterization of the e…

lcsh:Animal biochemistryMESH : AgedMESH : RodentiaMESH: RodentiaMESH: Base SequenceBiochemistryMESH: Lipid PeroxidationMESH : Information ServicesAntigen-Antibody ReactionsMESH: Health EducationEpitopesMESH: OrganizationsMESH: LibrariesMESH: Antigen-Antibody Reactionslcsh:QD415-436MESH: AnimalsMESH : OrganizationsMESH : Physician's RoleMESH: Bacterial ProteinsImmunosorbent Techniqueschemistry.chemical_classificationMESH: Conserved SequenceMethodology ArticleMESH : Computer Communication NetworksMESH: Chromatography AffinityMESH : Pseudomonas aeruginosaMESH : Chromatography AffinityMESH : Immunosorbent TechniquesMESH: Ethnic GroupsMESH : Ethnic GroupsMESH: EpitopesMESH : Patient SatisfactionMESH : United StatesMESH: MitochondriaMESH : Antigen-Antibody ReactionsMolecular Sequence DataMESH : Hydroxybutyrate DehydrogenaseMESH: Sequence AlignmentRodentiaMESH: Information ServicesMESH : Epitopeslcsh:BiochemistryMESH : Mitochondrial MembranesBacterial ProteinsMESH : Conserved SequenceComplementary DNAMESH : LibrariesMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Immunosorbent TechniquesMESH: Molecular Sequence DataMESH: HumansMESH : Consumer ParticipationMESH : HumansMESH: AdultMESH: Patient SatisfactionMESH: Hydroxybutyrate DehydrogenaseMESH: Consumer ParticipationchemistryLipid PeroxidationMESH: FemaleMESH: LiverMESH : Sequence Analysis DNAMESH: Continental Population GroupsMESH: Sequence Analysis DNAMESH : Molecular Sequence DataDehydrogenaseChromatography AffinityMESH: Mitochondrial MembranesMESH: Antibodies BacterialMESH : Bacterial ProteinsMESH : FemaleMESH: Computer Communication NetworksConserved SequenceMESH: AgedbiologyMESH : Lipid PeroxidationMESH : Sequence AlignmentMESH: Physician's RoleMESH : AdultAntibodies BacterialMitochondriaAmino acidLiverBiochemistryMitochondrial MembranesPseudomonas aeruginosaMESH: Pseudomonas aeruginosaMESH : MitochondriaMESH : Mass MediaMESH: Mass MediaMESH : MaleHydroxybutyrate DehydrogenaseAffinity chromatographyMESH : Health Education[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: United StatesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Antibodies Bacteriallcsh:QP501-801Jaculus orientalisMESH : Continental Population GroupsBase SequenceMESH : LiverSequence Analysis DNAbiology.organism_classificationMolecular biologyMESH: MaleEnzymePolyclonal antibodiesbiology.proteinMESH : Base SequenceNAD+ kinaseMESH : AnimalsSequence Alignment
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Prediction of Specific TCR-Peptide Binding From Large Dictionaries of TCR-Peptide Pairs

2019

Abstract The T cell repertoire is composed of T cell receptors (TCR) selected by their cognate MHC-peptides and naive TCR that do not bind known peptides. While the task of distinguishing a peptide-binding TCR from a naive TCR unlikely to bind any peptide can be performed using sequence motifs, distinguishing between TCRs binding different peptides requires more advanced methods. Such a prediction is the key for using TCR repertoires as disease-specific biomarkers. We here used large scale TCR-peptide dictionaries with state-of-the-art natural language processing (NLP) methods to produce ERGO (pEptide tcR matchinG predictiOn), a highly specific classifier to predict which TCR binds to which…

lcsh:Immunologic diseases. AllergyComputer scienceevaluation methodsT-LymphocytesT cellImmunologyReceptors Antigen T-CellEpitopes T-LymphocyteTarget peptidePeptide bindingPeptidechemical and pharmacologic phenomenaComputational biologyLigandsSoftware implementationautoencoder (AE)AntigenEvaluation methodsmedicineImmunology and AllergyHumansProtein Interaction Domains and MotifsEpitope specificityAntigensDatabases ProteinOriginal Researchchemistry.chemical_classificationBinding SitesT cell repertoireChemistryRepertoirelong short-term memory (LSTM)T-cell receptorepitope specificitydeep learninghemic and immune systemsmedicine.anatomical_structuremachine learningPeptidesSequence motiflcsh:RC581-607SoftwareProtein BindingSignal TransductionTCR repertoire analysisFrontiers in Immunology
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Quantitative Prediction of the Landscape of T Cell Epitope Immunogenicity in Sequence Space

2019

Immunodominant T cell epitopes preferentially targeted in multiple individuals are the critical element of successful vaccines and targeted immunotherapies. However, the underlying principles of this "convergence" of adaptive immunity among different individuals remain poorly understood. To quantitatively describe epitope immunogenicity, here we propose a supervised machine learning framework generating probabilistic estimates of immunogenicity, termed "immunogenicity scores," based on the numerical features computed through sequence-based simulation approximating the molecular scanning process of peptides presented onto major histocompatibility complex (MHC) by the human T cell receptor (T…

lcsh:Immunologic diseases. AllergyT cellT-LymphocytesImmunologyReceptors Antigen T-CellDatasets as TopicEpitopes T-Lymphocytechemical and pharmacologic phenomenaComputational biologyBiologyAdaptive ImmunityimmunogenicityMajor histocompatibility complexEpitopeMajor Histocompatibility ComplexmedicineImmunology and AllergyHumansComputer SimulationAntigen PresentationImmunodominant EpitopesRepertoireImmunogenicityT-cell receptorComputational BiologyAcquired immune systemmedicine.anatomical_structuremachine learningescape mutationbiology.proteinThermodynamicsT cell receptor repertoireSequence space (evolution)lcsh:RC581-607T cell epitopeFrontiers in Immunology
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The affinities of monoclonal antibodies against core antigen of hepatitis B virus

1994

Four monoclonal antibodies generated against the recombinant core antigen of hepatitis B virus are investigated for antigen binding. All exhibit a similar affinity to polystyrene-sorbed antigen but only one of them interacts with native form of HBcAg (an assembled particle) in solution. The presence of 0.1% sodium dodecylsulphate is required for the binding of other three antibodies. The phenomenon can be interpreted as inaccessibility of the corresponding epitopes unless the multimeric antigen structure is disrupted. The core antigen coated on polystyrene is considered as a similar exposed structure.

medicine.drug_classAntibody AffinityBiologyAntibodies Viralmedicine.disease_causeMonoclonal antibodyEpitopeEpitopesMiceAntigenVirologymedicineAnimalsHepatitis B virusHybridomasT-cell receptorAntibodies MonoclonalSodium Dodecyl SulfateGeneral Medicinebiology.organism_classificationHepatitis B Core AntigensVirologyMolecular biologyRecombinant ProteinsHBcAgHepadnaviridaebiology.proteinAntibodyArchives of Virology
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Monoclonal antibody 3H8: A useful tool in the diagnosis of candidiasis

1999

In a previous series of experiments six mAbs were obtained against cell wall extracts of Candida albicans ATCC 26555. After several studies only one of them, designated 3H8, has been used to produce a commercial kit for the rapid diagnosis of candidiasis, Bichro-latex albicans (Fomouze Diagnostics). The present study involved the generation and characterization of this mAb as an immunoglobulin G1 which recognizes mannoproteins of high molecular mass present in the C. albicans cell wall. ELISA assays showed that the presence of the epitope recognized by mAb 3H8 was similar in both yeast and mycelial cell walls of C. albicans, in contrast to the epitope for mAb 1B12, which is mainly expressed…

medicine.drug_classBiologyMonoclonal antibodyMicrobiologyEpitopeMicrobiologyCell wallEpitopesAntibody SpecificityCell WallmedicineHumansCandida albicansAntibodies Fungalchemistry.chemical_classificationCandidiasisAntibodies Monoclonalbiology.organism_classificationImmunohistochemistryYeastCorpus albicanschemistrybiology.proteinReagent Kits DiagnosticAntibodyGlycoprotein
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Analysis of liver-specific protein LSP using murine monoclonal antibodies.

1987

. We describe twenty murine monoclonal antibodies directed against different antigenic determinants of human and rabbit liver-specific protein LSP. Among them, nine were directed against liver-specific epitopes as judged from immunohistological studies. Immunoelectronmicroscopy revealed that seven of these monoclonals recognized membrane determinants differing in staining of distinct areas of the hepatocellular surface. Eleven antibodies were directed against intracellular structures. Western blot analysis showed that the epitopes detected were displayed on either single or multiple protein bands with apparent molecular weights between 24 000 and 60 000. Further differences were observed wi…

medicine.drug_classClinical BiochemistryMonoclonal antibodyBiochemistryEpitopeEpitopesMiceWestern blotAntigenmedicineAnimalsHumansbiologymedicine.diagnostic_testMolecular massAntibodies MonoclonalMembrane ProteinsProteinsGeneral MedicineMolecular biologyImmunohistochemistryStainingLiverAntigens Surfacebiology.proteinRabbitsAntibodyIntracellularEuropean journal of clinical investigation
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