Search results for "epitope"

showing 10 items of 455 documents

Immunoelectron microscopic observations on the inflammatory infiltrates and HLA antigens in hepatitis B and non-A, non-B.

1987

The present knowledge of the inflammatory reaction occurring in situ during hepatitis B favors a T cell-dependent MHC-restricted immune response. However, the reports in the literature are primarily based on the application of monoclonal antibodies directed at different lymphocyte subsets which discern only lymphocytic phenotypes and do not reflect the actual situation adequately. Therefore, we investigated the liver biopsies of patients with hepatitis B (28 patients) and non-A, non-B (21 patients) by immunoelectron microscopy with monoclonal antibodies directed at lymphocyte subtypes (pan-B, pan-T, T8, T4 and NKH1) and at activation epitopes (IL-2 receptor, TA1 and T11/3) as well, in order…

InflammationHepatologyHepatitis Viral Humanmedicine.drug_classLymphocyteImmunoelectron microscopyHuman leukocyte antigenHepatitis BBiologymedicine.diseaseMonoclonal antibodyHepatitis BHepatitis CEpitopeMicroscopy Electronmedicine.anatomical_structureImmune systemAntigenLiverHLA AntigensImmunologymedicineHumansLymphocytesHepatitis ChronicHepatology (Baltimore, Md.)
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Interleukin 4 suppresses primary interferon gamma response by T cells immunized in vivo and cultured in vitro with interleukin 2.

1996

This paper describes a novel primary in vivo/in vitro culture system which allows analysis of the effect of IL-4 added to culture 1 day after immunization on the production of IFN-gamma. Mice are immunized epicutaneously with picryl chloride (TNP) and draining lymph node cells were harvested 1 day later. These cells (1 day lymph node cells), when cultured in vitro for 3 days in the presence of IL-2, either continuously or as a pulse, give an IFN-gamma response on reexposure to antigen 3 days later. This production of IFN-gamma is both antigen-specific and genetically (MHC)-restricted and is due to both CD8+ and CD4+ T cells. However, if 1 day lymph node cells are cultured with both IL-2 and…

Interleukin 2MaleT-LymphocytesImmunologyMice Inbred StrainsPicryl ChlorideBiologyMajor histocompatibility complexBiochemistryPicryl chlorideMajor Histocompatibility Complexchemistry.chemical_compoundEpitopesInterferon-gammaMiceAntigenmedicineImmunology and AllergyAnimalsInterferon gammaMolecular BiologyLymph nodeInterleukin 4Cells CulturedHematologyMolecular biologyInterleukin-10Kineticsmedicine.anatomical_structurechemistryDepression ChemicalImmunologybiology.proteinInterleukin-2ImmunizationInterleukin-4Lymph NodesCD8medicine.drugCytokine
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T Cells Recognize an Immunodominant Epitope of Heat Shock Protein 65 in Kawasaki Disease

2000

Kawasaki disease (KD) is an acute systemic vasculitis of infancy and early childhood that is characterized by endothelial cell damage associated with T-cell activation. Lymphocytes infiltrating damaged tissues might be responsible for the disease through secretion of cytokines, such as tumor necrosis factor (TNF)-α, that could cause fever, as well as endothelial tissue damage. Debate is growing about the nature of antigen responsible for T-cell activation in KD. Bacillus Calmette Guerin (BCG) and purified protein derivative (PPD) hyper-responsiveness was observed in KD patients and this phenomenon was hypothetically ascribed to cross-reactivity between mycobacterial Heat Shock Protein (HSP)…

Interleukin 2medicine.medical_treatmentBiologyMolecular biologyEpitopeCytokineAntigenHeat shock proteinImmunologyGeneticsmedicineMolecular MedicineTumor necrosis factor alphaMolecular BiologyPeptide sequenceGenetics (clinical)CD8medicine.drugMolecular Medicine
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Revisiting CD8 T-cell ‘Memory Inflation’: New Insights with Implications for Cytomegaloviruses as Vaccine Vectors

2020

Murine models of cytomegalovirus (CMV) infection have revealed an exceptional kinetics of the immune response. After resolution of productive infection, transient contraction of the viral epitope-specific CD8 T-cell pool was found to be followed by a pool expansion specific for certain viral epitopes during non-productive &lsquo

KLRG10301 basic medicinecentral memory CD8 T cells (TCM)vaccine vectorHigh avidityImmunologylcsh:MedicineBiologyArticleEpitope03 medical and health sciences0302 clinical medicineImmune systemDrug DiscoveryCytotoxic T cellPharmacology (medical)Aviditycytomegalovirusmemory inflationPharmacologyeffector memory CD8 T cells (TEM)Human studiesEffectoravidity maturationlcsh:RVirology030104 developmental biologyInfectious Diseasesconventional TEM (cTEM)CD8inflationary TEM (iTEM)030215 immunologyVaccines
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Molecular mimicry may explain multi-organ damage in COVID-19

2020

International audience

Kawasaki vasculitiVascular damagemedicine.disease_causeEpitopes0302 clinical medicineOR7D4PandemicSevere acute respiratory syndrome coronavirus 2Immunology and AllergyComputingMilieux_MISCELLANEOUS0303 health sciencesLeukopenia[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]Molecular mimicryPARP9Cross ReactionEpitopemedicine.symptomCoronavirus InfectionsHuman2019-20 coronavirus outbreakCoronavirus disease 2019 (COVID-19)AnosmiaPneumonia ViralImmunologyAnosmiaCross ReactionsBiologyAutoimmune DiseaseArticleAutoimmune DiseasesBetacoronavirus03 medical and health sciencesKawasaki vasculitismedicineHumansPandemics030304 developmental biologyBetacoronaviruPandemicSARS-CoV-2Coronavirus InfectionModels ImmunologicalCOVID-19LeukopeniaMulti organbiology.organism_classificationVirologySLC12A6Molecular mimicry030217 neurology & neurosurgeryBetacoronavirusAutoimmunity Reviews
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Subcellular duplex DNA and G‐quadruplex interaction profiling of a hexagonal PtII metallacycle

2019

[Abstract] Metal‐driven self‐assembly afforded a multitude of fascinating supramolecular coordination complexes (SCCs) with applications as catalysts, host–guest, and stimuli‐responsive systems. However, the interest in the biological applications of SCCs is only starting to emerge and thorough characterization of their behavior in biological milieus is still lacking. Herein, we report on the synthesis and detailed in‐cell tracking of a Pt2L2 metallacycle. We show that our hexagonal supramolecule accumulates in cancer cell nuclei, exerting a distinctive blue fluorescence staining of chromatin resistant to UV photobleaching selectively in nucleolar G4‐rich regions. SCC co‐localizes with epit…

KeratinocytesModels MolecularOrganoplatinum CompoundsmetallacycleSupramolecular chemistry010402 general chemistryG-quadruplex01 natural sciencesCatalysisEpitopeMetallacycleCell Line Tumorsubcellular localizationHumansplatinumPlatinumG-quadruplex010405 organic chemistryHexagonal crystal systemChemistrySubcellular localizationCommunicationDNAGeneral ChemistryFibroblastsMetallacycleSubcellular localizationPhotobleachingCommunicationsSCC0104 chemical sciencesChromatinG-QuadruplexesSettore CHIM/03 - Chimica Generale E InorganicaMCF-7 CellsBiophysicsSpectrophotometry Ultraviolet
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Identification of an endothelial cell binding site on kininogen domain D3

1995

High and low molecular mass kininogen, two multidomain plasma proteins, bind to endothelial cells, platelets, and neutrophils in the intravascular compartment. The specific cell attachment site on their common heavy chain is mediated by domain-3, a cystatin-like structure with inhibitory capacity for papain-like proteinases (Jiang, Y., Müller-Esterl, W., and Schmaier, A. H. (1992) J. Biol. Chem. 267, 3712-3717). In this report, the domain-3 cell binding site is determined by an antibody-directed strategy. The epitope of monoclonal antibody HKH15, which binds to domain-3 and blocks the binding of kininogens to platelets and endothelial cells, was mapped using seven synthetic peptides, which …

Kininogen bindingBlotting WesternMolecular Sequence DataBiotinBinding CompetitiveBiochemistryEpitopeEpitopesHumansAmino Acid SequenceBinding siteMolecular BiologyKininogenBinding SitesMolecular massKininogensChemistryAntibodies MonoclonalCell BiologyMolecular biologyEndothelial stem cellBiochemistryBiotinylationEndothelium VascularCystatinPeptidesJournal of Biological Chemistry
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Mapping of the high molecular weight kininogen binding site of prekallikrein. Evidence for a discontinuous epitope formed by distinct segments of the…

1993

Prekallikrein, a glycoprotein involved in contact phase activation, circulates in plasma in the form of a binary complex with high molecular weight kininogen (H-kininogen). The binding to H-kininogen is mediated by the prekallikrein heavy chain consisting of four repetitive domains, A1-A4. To define more precisely the region(s) involved in kininogen binding, we have employed an affinity cross-linking strategy with a synthetic peptide of 31 residues which mimics the prekallikrein binding site of H-kininogen. Cross-linking of the radiolabeled peptide to (pre)kallikrein revealed a binding segment in the NH2-terminal portion of the prekallikrein heavy chain; another binding segment was located …

Kininogen bindingHigh-molecular-weight kininogenMacromolecular SubstancesMolecular Sequence DataEnzyme-Linked Immunosorbent AssayBiochemistryBinding CompetitiveIodine RadioisotopesHigh molecular weight kininogen bindingEpitopesZymogenHumansAmino Acid SequenceBinding siteMolecular BiologyKininogenBinding SitesChemistryKininogensPrekallikreinPrekallikreinCell BiologyKallikreinPeptide FragmentsModels StructuralMolecular WeightKineticsBiochemistryAutoradiographyElectrophoresis Polyacrylamide GelPeptidescirculatory and respiratory physiology
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Mapping of the Discontinuous Kininogen Binding Site of Prekallikrein

1996

Prekallikrein, the precursor to the serine proteinase kallikrein, circulates in plasma in an equimolar complex with H-kininogen. The binding to H-kininogen is mediated by the kallikrein heavy chain consisting of four "apple" domains, A1-A4, which attaches to H-kininogen with high specificity and affinity (KD = 83 nM). At least two distinct portions of the kallikrein heavy chain form this H-kininogen binding site: a proximal segment located in the NH2-terminal fragment of the heavy chain encompassing A1, and distal segment(s) located in COOH-terminal fragment spanning domains A2-A4. The proximal binding segment has been located to amino acid positions 56-86 of A1. To precisely map the distal…

Kininogen bindingchemistry.chemical_classificationChemistryPrekallikreinCell BiologyKallikreinBiochemistryMolecular biologyEpitopelaw.inventionAmino acidSerinelawRecombinant DNABinding siteMolecular Biologycirculatory and respiratory physiologyJournal of Biological Chemistry
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Monoclonal anti-fosB antibody specific for predetermined, nonstructural region of the fosB protein.

1997

Comparison of the primary structures and theoretical prediction of the potential antigenic determinant of the deduced Fos proteins reveals the presence of a nonstructural and hydrophilic region juxtaposed to the leucine zipper and nonconserved among the Fos protein family. To develop monoclonal anti-peptide antibodies capable of distinguishing all Fos-proteins, synthetic peptides specific for the mentioned predicted region were synthesized manually by the "tea-bag" method. Immunization of Balb/c mice with fosB-related synthetic peptide BSA gave rise to mouse hybridoma cell line K21 (IgG1, kappa) secreting highly specific antibodies against corresponding human fosB protein. Fine mapping of t…

Leucine zippermedicine.drug_classImmunologyMolecular Sequence DataEnzyme-Linked Immunosorbent AssayMonoclonal antibodyEpitopeMiceAntibody SpecificityGeneticsmedicineAnimalsHumansAmino Acid SequencePeptide sequencebiologyProtein primary structureDrug Resistance MicrobialMolecular biologyPeptide FragmentsEpitope mappingbiology.proteinAntibodyProto-Oncogene Proteins c-fosEpitope MappingFOSBHybridoma
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