Search results for "epitope(s)"

showing 10 items of 254 documents

Influence of antibody binding on oxygen binding behavior of Panulirus interruptus hemocyanin

1997

Oxygen binding behavior of monomeric subunit a and the hexameric form of this subunit of hemocyanin of Panulirus interruptus is influenced by the binding of various monoclonal antibodies. These antibodies react with other surface parts of the subunit than its second domain in which the oxygen binding site is located. The influence of three monoclonal antibodies and their antigen binding fragments (F-ab) has been investigated. Two antibodies increase the oxygen affinity of monomeric hemocyanin from that observed in its low affinity T-state, while the third has little influence on this property. F-ab fragments abolish almost completely the cooperativity of oxygen binding by the hexameric hemo…

Protein ConformationStereochemistrymedicine.drug_classProtein subunitmedicine.medical_treatmentcooperativityBiophysicsCooperativityPlasma protein bindingmacromolecular substancesMonoclonal antibodyBiochemistryEpitopesImmunoglobulin Fab FragmentsProtein structureSUBUNIT-AStructural BiologyAMINO-ACID SEQUENCEGeneticsmedicineAnimalsCRYSTAL-STRUCTUREMolecular BiologyPanulirus interruptusChemistryImmunoglobulin Fab FragmentsAntibodies MonoclonalHemocyaninCell BiologyNephropidaeOxygenBiochemistryRESOLUTIONHemocyaninsoxygen bindingmonoclonal antibodieshemocyaninOxygen bindingProtein Binding
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Immunological analyses of human papillomavirus capsids

2001

Recombinant human papillomavirus (HPV) virus-like particles (VLPs) are promising vaccine candidates for controlling anogenital HPV disease. Questions remain, however, concerning the extent of capsid antigenic similarity between closely related virus genotypes. To investigate this issue, we produced VLPs and corresponding polyclonal immune sera from several anogenital HPV types, and examined these reagents in enzyme-linked immunosorbent assays (ELISAs) and in cross-neutralization studies. Despite varying degrees of L1 genetic sequence relatedness, VLPs of each type examined induced high-titer serum polyclonal antibody responses that were entirely genotype-specific. In an in vitro infectivity…

Protein DenaturationGenotypeProtein ConformationvirusesEnzyme-Linked Immunosorbent AssayVaccinia virusCross ReactionsBiologyAntibodies ViralRecombinant virusEpitopeVirusAbsorptionEpitopesCapsidVirus-like particleAntibody SpecificityNeutralization TestsAntigenic variationHumansSerotypingAntigens ViralPapillomaviridaeAntiserumVaccines SyntheticGeneral VeterinaryGeneral Immunology and MicrobiologyImmune SeraViral VaccinePublic Health Environmental and Occupational HealthAntibodies Monoclonalvirus diseasesViral VaccinesVirologyInfectious DiseasesCapsidMolecular MedicineVaccine
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Heparan sulfate proteoglycans interact exclusively with conformationally intact HPV L1 assemblies: basis for a virus-like particle ELISA.

2004

In this article, we demonstrate that interaction of human papillomavirus-like particles (HPV-VLPs) with the putative glucosaminoglycan binding receptor is strictly dependent on conformational integrity. Such conformations are present on VLPs and capsomeres but not on monomers of the major capsid protein, L1, confirming reports that capsomeres can induce virus-neutralizing antibodies. Furthermore, we show the suitability of this specific interaction for development of VLP-based enzyme-linked immunosorbent assays (ELISAs), using heparin for indirect coupling of VLPs to microtiter plates, which may add an intrinsic quality control. This avoids presentation of linear, often highly cross-reactiv…

Protein DenaturationProtein ConformationvirusesEnzyme-Linked Immunosorbent AssayPlasma protein bindingCross ReactionsAntibodies ViralEpitopeEpitopesProtein structureVirus-like particleNeutralization TestsVirologyCentrifugation Density GradientHumansPapillomaviridaeGlycosaminoglycansbiologyHeparinCapsomerevirus diseasesOncogene Proteins ViralVirologyInfectious DiseasesProteoglycanCapsidbiology.proteinReceptors VirusCapsid ProteinsHeparan Sulfate ProteoglycansConformational epitopeProtein BindingJournal of medical virology
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Processing requirements for the recognition of insulin fragments by murine T cells.

1988

In this study we investigated aspects of antigen processing using insulin and insulin A chain-derived fragments as model antigens in Ab alpha Ak beta-restricted T-cell stimulation. Similarly to other proteins, the immunodominant region of insulin recognized by these T cells is limited in size. It is located on the insulin A chain and encompasses a portion of the molecule that is represented faithfully by peptide A1-14(SSO3-)3. Efficient presentation of intact insulin and its entire A chain is dependent on uptake and processing by APC. Whereas peptides stemming from various globular proteins are known to be presented to T cells by APC without requiring processing, this is not the case with A…

Protein Denaturationmedicine.medical_treatmentT-LymphocytesImmunologyReceptors Antigen T-CellAntigen-Presenting CellsPeptideLymphocyte ActivationMajor Histocompatibility Complexchemistry.chemical_compoundEpitopesAntigenmedicineImmunology and AllergyAnimalsInsulinchemistry.chemical_classificationMHC class IIbiologyAntigen processingInsulinT-cell receptorTunicamycinClone CellsRatsBiochemistrychemistrybiology.proteinInsulin processingImmunological reviews
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Insights in ChAdOx1 nCoV-19 vaccine-induced immune thrombotic thrombocytopenia

2021

Abstract SARS-CoV-2 vaccine ChAdOx1 nCoV-19 (AstraZeneca) causes a thromboembolic complication termed vaccine-induced immune thrombotic thrombocytopenia (VITT). Using biophysical techniques, mouse models, and analysis of VITT patient samples, we identified determinants of this vaccine-induced adverse reaction. Super-resolution microscopy visualized vaccine components forming antigenic complexes with platelet factor 4 (PF4) on platelet surfaces to which anti-PF4 antibodies obtained from VITT patients bound. PF4/vaccine complex formation was charge-driven and increased by addition of DNA. Proteomics identified substantial amounts of virus production-derived T-REx HEK293 proteins in the ethyle…

ProteomicsAntigen-Antibody ComplexPlatelet Factor 4Extracellular TrapsBiochemistryEpitopesMiceSinus Thrombosis IntracranialMedicinePlateletCell Line TransformedMicroscopybiologyHematologymedicine.anatomical_structureSpike Glycoprotein CoronavirusAntibodyDrug ContaminationVirus CultivationGenetic VectorsImmunologyAdenoviridaeProinflammatory cytokineImaging Three-DimensionalImmune systemAntigenChAdOx1 nCoV-19AnimalsHumansPlatelet activationB cellAutoantibodiesInflammationPurpura Thrombocytopenic IdiopathicSARS-CoV-2business.industryCOVID-19Cell BiologyPlatelet ActivationPlatelets and ThrombopoiesisDynamic Light ScatteringHEK293 CellsImmunoglobulin GImmunologybiology.proteinCapsid ProteinsbusinessCapillary Leak SyndromePlatelet factor 4Extravasation of Diagnostic and Therapeutic MaterialsBlood
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HIV plays (and wins) a game of T cell Brinkmanship.

2013

HIV, unlike other viruses, may benefit from immune recognition by preserving the sequence of its T cell epitopes, thereby enhancing transmission between cells.

QH301-705.5T cellImmunologyEpitopes T-LymphocyteHIV InfectionsMicrobiologyGeneral Biochemistry Genetics and Molecular BiologyEpitopeVirusViral EvolutionImmune systemAntigenImmunodeficiency VirusesVirologymedicineCytotoxic T cellHumansComputer SimulationBiology (General)BiologyImmune EvasionEvolutionary BiologyGeneral Immunology and MicrobiologybiologyGeneral NeuroscienceViral Immune Evasionbiochemical phenomena metabolism and nutritionAcquired immune systemVirologymedicine.anatomical_structureImmunologybiology.proteinHIV-1AntibodyGeneral Agricultural and Biological SciencesResearch ArticlePLoS biology
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The Ability of Variant Peptides to Reverse the Nonresponsiveness of T Lymphocytes to the Wild-Type Sequence p53264–272 Epitope

2002

Abstract Recently, we observed that CTL specific for the wild-type (wt) sequence p53264–272 peptide could only be expanded ex vivo from PBMC of a subset of the HLA-A2.1+ normal donors or cancer patients tested. Surprisingly, the tumors of the responsive patients expressed normal levels of wt p53 and could be considered unlikely to present this epitope. In contrast, tumors of nonresponsive patients accumulated mutant p53 and were more likely to present this epitope. We sought to increase the responsive rate to the wt p53264–272 peptide of PBMC obtained from normal donors and patients by identifying more immunogenic variants of this peptide. Two such variants were generated by amino acid exch…

Receptors Antigen T-Cell alpha-betaT cellImmunologyAntigen presentationEpitopes T-LymphocytePeptideBiologyLymphocyte ActivationEpitopeT-Lymphocyte SubsetsHLA-A2 AntigenImmune ToleranceTumor Cells CulturedmedicineHumansImmunology and AllergyGene Rearrangement beta-Chain T-Cell Antigen ReceptorCells CulturedMouth neoplasmchemistry.chemical_classificationAntigen PresentationT-cell receptorWild typeCytotoxicity Tests ImmunologicVirologyPeptide FragmentsCTL*medicine.anatomical_structureAmino Acid SubstitutionchemistryCarcinoma Squamous CellLeukocytes MononuclearMouth NeoplasmsTumor Suppressor Protein p53Protein BindingT-Lymphocytes CytotoxicThe Journal of Immunology
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Human leucocyte antigen-A2 restricted and Mycobacterium tuberculosis 19-kDa antigen-specific CD8+ T-cell responses are oligoclonal and exhibit a T-ce…

2001

CD8+ T cells can be grouped into two different types of secretory T lymphocytes, based on the cytokine-secretion pattern upon antigen exposure: those with a T-cell cytotoxic type 1 response (Tc1), which secrete interferon-gamma (IFN-gamma), or those with a T-cell cytotoxic type 2 response, which secrete interleukin (IL)-4 and IL-10. We examined the CD8+ T-cell response directed against an immunodominant human leucocyte antigen (HLA)-A2-presented peptide derived from a 19-kDa Mycobacterium tuberculosis-associated antigen. T cells were examined by functional analysis and by T-cell receptor (TCR) complementarity-determining region 3 (CDR3)-spectratyping, which defines the complexity of a T-cel…

Receptors Antigen T-Cell alpha-betaT cellImmunologyHuman leukocyte antigenCD8-Positive T-LymphocytesBiologyLymphocyte ActivationEpitopeCell LineInterferon-gammaAntigenHLA-A2 AntigenmedicineHumansImmunology and AllergyCytotoxic T cellAntigen-presenting cellTuberculosis PulmonaryAntigens BacterialImmunodominant EpitopesT-cell receptorGranulocyte-Macrophage Colony-Stimulating FactorMycobacterium tuberculosisOriginal ArticlesComplementarity Determining RegionsMolecular biologyPeptide FragmentsClone Cellsmedicine.anatomical_structureImmunologyInterleukin-4CD8Immunology
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Cross-Reactivity of Antibodies Immunoadsorbed to Laminin with Recombinant Human La (SS-B) Protein

1998

Anti-La (SS-B) antibodies cross-reacting with mouse B1 laminin were reported in sera of patients with systemic lupus erythematosus. However, the common epitope had not been characterized. Immunoblotting conditions were established, allowing detection and elution of anti-La (SS-B)/laminin cross-reacting antibodies. Antibodies adsorbed to mouse B1 laminin represented a subclass of anti-La antibodies. They strongly reacted with human full length recombinant La protein. However, they failed to react with either an N-terminal La peptide consisting of amino acids 1-192 or a C-terminal La peptide starting at methionine 223, while they still reacted with recombinant La peptides consisting of the am…

Recombinant Fusion ProteinsMolecular Sequence DataImmunologyPeptideCross ReactionsBiologyAutoantigensEpitopeAutoimmune Diseaseslaw.inventionEpitopesMiceSpecies SpecificityAntigenAntibody SpecificitylawLamininConsensus SequenceAnimalsHumansImmunology and AllergyAmino Acid SequenceElméleti orvostudományokPeptide sequenceImmunosorbent TechniquesAutoantibodieschemistry.chemical_classificationOrvostudományokMolecular biologyPeptide FragmentsAmino acidRibonucleoproteinschemistryRecombinant DNAbiology.proteinKidney DiseasesLamininAntibodyJournal of Autoimmunity
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DRB1*0401-restricted human T cell clone specific for the major proinsulin73-90 epitope expresses a down-regulatory T helper 2 phenotype.

2006

Recently, we have identified proinsulin (P-Ins) 73-90 as an immunodominant T cell epitope of HLA-DRB1*0401 (DR4) subjects with β-islet cell autoimmunity and of HLA-DR4/CD4 double-transgenic mice immunized with human P-Ins. We have compared the fine specificities of one human CD4 T cell clone and two mouse T cell hybridoma clones recognizing this epitope, and, although these three clones all recognized the same core region (LALEGSLQK), there were major differences in how they interacted with the peptide (p)/HLA complex, reflecting the fact that human P-Ins is a foreign antigen in the mouse and an autoantigen in the type 1 diabetes patient. The human T cell clone was forkhead transcription f…

Regulatory T cellT cellT-LymphocytesMolecular Sequence DataClone (cell biology)Mice TransgenicHuman leukocyte antigenBiologyEpitopeEpitopesMiceAntigenT-Lymphocyte SubsetsmedicineCytotoxic T cellAnimalsHumansAmino Acid SequenceAmino AcidsMultidisciplinaryFOXP3Forkhead Transcription FactorsHLA-DR AntigensBiological SciencesMolecular biologyPeptide Fragmentsmedicine.anatomical_structurePhenotypeHLA-DRB1 ChainsProinsulinProceedings of the National Academy of Sciences of the United States of America
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