Search results for "Epitope mapping"

showing 10 items of 28 documents

Fasciola spp: Mapping of the MF6 epitope and antigenic analysis of the MF6p/HDM family of heme-binding proteins

2017

MF6p/FhHDM-1 is a small cationic heme-binding protein which is recognized by the monoclonal antibody (mAb) MF6, and abundantly present in parenchymal cells and secreted antigens of Fasciola hepatica. Orthologs of this protein (MF6p/HDMs) also exist in other causal agents of important foodborne trematodiasis, such as Clonorchis sinensis, Opisthorchis viverrini and Paragonimus westermani. Considering that MF6p/FhHDM-1 is relevant for heme homeostasis in Fasciola and was reported to have immunomodulatory properties, this protein is expected to be a useful target for vaccination. Thus, in this study we mapped the epitope recognized by mAb MF6 and evaluated its antigenicity in sheep. The sequenc…

0301 basic medicineParagonimus westermaniFasciola sppPhysiologyProtein ConformationFlatwormslcsh:MedicineProtein Structure PredictionBiochemistryEpitopeAntigenicEpitopes0302 clinical medicineAnimal CellsImmune PhysiologyMedicine and Health SciencesMacromolecular Structure AnalysisMF6p/HDMEnzyme-Linked Immunoassayslcsh:ScienceMammalsNeuronsImmune System ProteinsMultidisciplinaryFasciolabiologyVaccinationEukaryotaAntibodies MonoclonalRuminantsDendritic StructureVertebratesCellular TypesAntibodyResearch ArticleHemeproteinsProtein StructureAntigenicityFascioliasisHeme bindingImmunology030231 tropical medicineAntibodies HelminthEnzyme-Linked Immunosorbent AssayHemeResearch and Analysis MethodsTrematodesAntibodiesHeme-Binding Proteins03 medical and health sciencesHelminthsparasitic diseasesParasitic DiseasesFasciola hepaticaAnimalsImmunoassaysMolecular BiologySheeplcsh:ROrganismsBiology and Life SciencesProteinsCell BiologyDendritesNeuronal DendritesFasciola hepaticabiology.organism_classificationInvertebratesMolecular biologyFasciola030104 developmental biologyEpitope mappingCellular NeuroscienceAntigens HelminthAmniotesImmunologic Techniquesbiology.proteinlcsh:QCarrier ProteinsEpitope MappingNeuroscience
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Characterization of target antigens from anti-neutrophil cytoplasmic antibodies in autoimmune hepatitis type-I.

1997

The occurrence of anti-neutrophil cytoplasmic antibodies (ANCA) has been described in sera of patients with autoimmune hepatitis (AIH). The significance of this finding remains uncertain and the nature of the target antigen(s) has not yet been defined. We studied 32 sera from patients with AIH type-I and prepared extracts of human neutrophils to identify the target antigen(s). A 43 kDa dominant immunoreactive protein was found and identified as the cytoskeletal component actin. Initial studies to define the antigenic determinants identified three different actin domains.

AdultMaleNeutrophilsClinical BiochemistryBlotting WesternMolecular Sequence DataFluorescent Antibody TechniqueAutoimmune hepatitisBiologyBiochemistryAnalytical ChemistryAntibodies Antineutrophil CytoplasmicAutoimmune DiseasesHepatitisEpitopesAntigenimmune system diseasesmedicineTumor Cells CulturedAnimalsHumansAmino Acid SequenceAntigensCytoskeletonAnti-neutrophil cytoplasmic antibodyAgedAged 80 and overMiddle Agedmedicine.diseaseRatsBlotEpitope mappingCytoplasmImmunologybiology.proteinFemaleAntibodyElectrophoresis
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Generation of monoclonal antibodies against human regulatory T cells.

2009

Abstract Natural CD4 + CD25 + Foxp3 + regulatory T cells (Tregs) control the activation of the immune system and therefore have become a major area of research in immunology. The generation of monoclonal antibodies against human Tregs offers the possibility to discover novel Treg-specific or Treg-associated surface markers and to identify targets for a therapeutic modulation of Tregs. Here we present a methodology optimized to efficiently induce and select mAb against human Tregs by repeated immunization of mice with Tregs from a single donor and a differential two-step flow cytometry-based hybridoma screening procedure.

Anticorps monoclonalmedicine.drug_classImmunologyReceptors Antigen T-Cellchemical and pharmacologic phenomenaCell SeparationBiologyMonoclonal antibodyT-Lymphocytes RegulatoryFlow cytometryEpitopesMiceImmune systemAntibody SpecificitymedicineImmunology and AllergyAnimalsHumansIL-2 receptorLeukapheresisImmunization ScheduleHybridomasmedicine.diagnostic_testInterleukin-2 Receptor alpha SubunitFOXP3Antibodies Monoclonalhemic and immune systemsForkhead Transcription FactorsT lymphocyteFlow CytometryImmunizationImmunologyFemaleEpitope MappingJournal of immunological methods
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Precise mapping of the Goodpasture epitope(s) using phage display, site-directed mutagenesis, and surface plasmon resonance.

2013

Goodpasture disease is an autoimmune disorder mediated by circulating autoantibodies against the noncollagenous-1 (NC1) domain of the alpha 3 chain of type IV collagen (alpha 3(IV)NC1). The structure of Goodpasture epitope(s) has been previously mapped into two main binding regions (E-A and E-B) of the alpha 3(IV)NC1 domain using a residue mutation approach on the highly related alpha 1(IV)NC1 domain. Here we combined phage display and surface plasmon resonance technology to more precisely localize the pathogenic binding sites. Peptides mimicking the Goodpasture epitope(s) were used to identify residues involved in autoantibody binding and found involvement of eight residues previously unre…

Collagen Type IVMalePhage displayautoantibodiesMutantMutagenesis (molecular biology technique)Enzyme-Linked Immunosorbent Assaycollagen type IVAutoantigensEpitopeType IV collagenHumansBinding siteSite-directed mutagenesisAutoantibodiesepitopeChemistryAutoantibodyGoodpasture diseaseMiddle AgedSurface Plasmon ResonanceMolecular biologyNephrologyMutagenesis Site-DirectedBinding Sites Antibodyphage displayCell Surface Display Techniquessurface plasmon resonanceEpitope MappingKidney international
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The development of synthetic antitumour vaccines from mucin glycopeptide antigens.

2013

Based on important cell-biological and biochemical results concerning the structural difference between membrane glycoproteins of normal epithelial cells and epithelial tumour cells, tumour-associated glycopeptide antigens have been chemically synthesised and structurally confirmed. Glycopeptide structures of the tandem repeat sequence of mucin MUC1 of epithelial tumour cells constitute the most promising tumour-associated antigens. In order to generate a sufficient immunogenicity of these endogenous structures, usually tolerated by the immune system, these synthetic glycopeptide antigens were conjugated to immune stimulating components: in fully synthetic two-component vaccines either with…

DendrimersVaccines SyntheticChemistryImmunogenicityT-LymphocytesMucin-1ToxoidGeneral ChemistryCancer VaccinesEpitopeGlycopeptideAntibodiesImmune systemEpitope mappingAntigenNeoplasmsImmunologyTetanus ToxoidAnimalsHumansMUC1Epitope MappingChemical Society reviews
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Characterization of murine monoclonal antibodies against the Ro52 autoantigen

1997

SUMMARY Immunization of BALB/c mice with purified recombinant human Ro52 protein resulted in three anti-Ro52 MoAbs termed 2E7, 4C6 and 4F11. All anti-Ro52 MoAbs specifically reacted with recombinant human Ro52 protein, and also with Ro52 protein in total extracts of all human cell lines analysed, including the epithelial cell line HeLa, the B cell line Raji, the bladder carcinoma cell line RT112, and a fibroblast cell line derived from patients with xeroderma pigmentosum. The anti-Ro52 MoAbs were able to immunoprecipitate the recombinant human Ro52 protein expressed in wheat germ extract, but failed to precipitate hY RNAs from cell extracts. The staining pattern of the MoAbs strongly differ…

Editorial Reviewmedicine.drug_classMolecular Sequence DataImmunologyCellMonoclonal antibodyAutoantigensEpitopelaw.inventionHeLaMiceAntibody SpecificitylawRNA Small CytoplasmicmedicineAnimalsHumansImmunology and AllergyAmino Acid SequencebiologyAntibodies Monoclonalbiology.organism_classificationMolecular biologyRecombinant ProteinsStainingEpitope mappingmedicine.anatomical_structureRibonucleoproteinsImmunologybiology.proteinRecombinant DNAAntibodySequence AlignmentEpitope MappingGene DeletionClinical and Experimental Immunology
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Fine-mapping of the B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen

2002

In this study, we report the exact localization and substitutional characterization of a B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen. A set of deletion variants containing preS2 sequences of different length was generated on the basis of frCP as a carrier. It was found after Western blot analysis that three monoclonal antibodies (MAbs) (2-11B1, 3-11C2, HB.OT10) recognized the linear preS2 sequence within the amino acid (aa) stretch 3-WNSTTFHQTLQDP-13. The importance of each aa residue of the epitope was proved by comparison of antibody binding to alanine-substituted peptides in both free-peptide and Pepscan variants.

HBsAgmedicine.drug_classBlotting WesternMolecular Sequence DataImmunologyMonoclonal antibodyEpitopeMiceViral Envelope ProteinsmedicineAnimalsImmunology and AllergyAmino Acid SequenceProtein PrecursorsPeptide sequenceHepatitis B Surface AntigensLinear epitopebiologyAntibodies MonoclonalMolecular biologyEpitope mappingPepscanbiology.proteinEpitopes B-LymphocyteAntibodyEpitope MappingJournal of Immunological Methods
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Immune activation promotes evolutionary conservation of T-cell epitopes in HIV-1.

2013

The immune system should constitute a strong selective pressure promoting viral genetic diversity and evolution. However, HIV shows lower sequence variability at T-cell epitopes than elsewhere in the genome, in contrast with other human RNA viruses. Here, we propose that epitope conservation is a consequence of the particular interactions established between HIV and the immune system. On one hand, epitope recognition triggers an anti-HIV response mediated by cytotoxic T-lymphocytes (CTLs), but on the other hand, activation of CD4(+) helper T lymphocytes (TH cells) promotes HIV replication. Mathematical modeling of these opposite selective forces revealed that selection at the intrapatient l…

Helper T lymphocyteQH301-705.5HIV AntigensEpitopes T-LymphocyteHIV InfectionsImmunodominanceBiologyVirus ReplicationGeneral Biochemistry Genetics and Molecular BiologyEpitopeEvolution Molecular03 medical and health sciencesImmune systemCytotoxic T cellHumansComputer SimulationAmino Acid SequenceBiology (General)BiologyConserved Sequence030304 developmental biologyImmune Evasion0303 health sciencesImmunity CellularGeneral Immunology and MicrobiologyModels Genetic030306 microbiologyGeneral NeuroscienceGenetic VariationViral LoadVirology3. Good healthEpitope mappingHIV AntigensViral replicationImmunologyHost-Pathogen InteractionsSynopsisHIV-1General Agricultural and Biological SciencesAlgorithms
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N-terminal myristoylation-dependent masking of neutralizing epitopes in the preS1 attachment site of hepatitis B virus

2011

The N-terminally myristoylated preS1 domain of the large hepatitis B surface protein (LHBs) mediates specific attachment of hepatitis B virus (HBV) to hepatocytes. Its B-cell epitopes leading to neutralization of infectivity are not yet characterized.We inserted C- and N-terminal preS1 peptides into the most immunogenic region of HBV core particles, therewith immunized Balb/c mice and determined binding properties and neutralization potential of resulting antibodies in vitro.The particles with preS1 inserts were highly immunogenic and the corresponding anti-preS antibodies strongly bound to HBV particles from chronic carriers infected with different HBV genotypes A-F. However, antibodies bi…

Hepatitis B virusHBsAgGenotypeMolecular Sequence DataIn Vitro TechniquesBiologymedicine.disease_causeMyristic AcidNeutralizationEpitopeMice03 medical and health sciencesHepatitis B Chronic0302 clinical medicinemedicineAnimalsHumansHepatitis B VaccinesAmino Acid SequenceHepatitis B AntibodiesProtein Precursors030304 developmental biologyHepatitis B virusInfectivityMice Inbred BALB C0303 health sciencesBinding SitesHepatitis B Surface AntigensSequence Homology Amino AcidHepatologyHepatitis Bmedicine.diseaseAntibodies NeutralizingVirology3. Good healthEpitope mappingbiology.proteinEpitopes B-Lymphocyte030211 gastroenterology & hepatologyAntibodyEpitope MappingJournal of Hepatology
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Impact of MHC class I alleles on the M. tuberculosis antigen-specific CD8+ T-cell response in patients with pulmonary tuberculosis

2007

Challenged by scattered understanding of protective immunity to Mycobacterium tuberculosis (MTB), we have mapped peptide epitopes to human leukocyte antigen (HLA)-A*0101, A*0201, A*1101, A*2402, B*0702, B*0801 and B*1501 of the secreted mycobacterial antigen Ag85B, a vaccine candidate that may be associated with immune protection. Affinity (ED(50)) and half-life (t(1/2), off-rate) analysis for individual peptide species on HLA-A and HLA-B molecules revealed binding ranges between 10(-3) and 10(-7) M. After selection of the best matches, major histocompatibility complex class I/peptide tetramer complexes were constructed to measure the CD8+ T-cell responses directly ex vivo in peripheral blo…

ImmunologyGenes MHC Class IPeptide bindingHuman leukocyte antigenCD8-Positive T-LymphocytesMajor histocompatibility complexEpitopeMycobacterium tuberculosisMHC class IGeneticsHumansCytotoxic T cellTuberculosis PulmonaryAllelesCells CulturedGenetics (clinical)HLA-A AntigensbiologyMycobacterium tuberculosisFlow Cytometrybiology.organism_classificationVirologyMolecular biologyHLA-B Antigensbiology.proteinEpitope MappingCD8Genes & Immunity
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