Search results for "epitope"

showing 10 items of 455 documents

Properties of modified hepatitis B virus surface antigen particles carrying preS epitopes

1995

The current hepatitis B virus (HBV) vaccines contain the small (S) and middle (M) viral envelope proteins in particulate form but lack the large (L) protein. Although these particles elicit protective immunity to HBV, inclusion of the immunogenic preS1 region of the L protein may enhance their efficacy. To present preS1-derived epitopes on secretable subviral particles we rearranged the HBV envelope ORF by fusing part or all of the preS1 region to either the N or C terminus of the S protein. Fusion of the first 42 residues of preS1 to either site allowed efficient secretion of the modified particles and rendered the linked sequence accessible at the surface of the particle. Conversely, fusi…

Signal peptideHepatitis B virusAntigenicityMyeloma proteinHeterologousmedicine.disease_causeEpitopeCell LineEpitopesMiceViral Envelope ProteinsViral envelopeVirologymedicineAnimalsHumansHepatitis B VaccinesCloning MolecularProtein PrecursorsHepatitis B virusMice Inbred BALB CVaccines SyntheticHepatitis B Surface AntigensbiologyVirionVirologyMolecular biologybiology.proteinAntibodyJournal of General Virology
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UV Exposure Boosts Transcutaneous Immunization and Improves Tumor Immunity: Cytotoxic T-Cell Priming through the Skin

2010

Immunologic approaches to combat cancer aim at the induction of tumor-reactive immune responses to achieve long-term protection. In this context, we recently developed a transcutaneous immunization (TCI) method using the Toll-like receptor (TLR) 7 agonist imiquimod and a peptide epitope. Application onto intact skin induces potent cytotoxic T lymphocyte (CTL) responses and protection against transplanted tumors. The purpose of this study was to explore the effects of UV irradiation on imiquimod-based TCI. Here we show that skin exposure to low-dose UV light before TCI with imiquimod strongly boosts specific CTL responses leading to memory formation and enhanced tumor protection. Toward the …

Skin NeoplasmsUltraviolet RaysPriming (immunology)ImiquimodAntineoplastic AgentsDermatologyBiochemistryEpitopeMiceImmune systemImmune ToleranceCytotoxic T cellMedicineAnimalsReceptorMolecular BiologySkinImiquimodMembrane GlycoproteinsDose-Response Relationship Drugbusiness.industryDose-Response Relationship RadiationCell BiologyMice Mutant StrainsVaccinationMice Inbred C57BLCTL*Toll-Like Receptor 7Langerhans CellsImmunologyAminoquinolinesbusinessImmunologic Memorymedicine.drugT-Lymphocytes CytotoxicJournal of Investigative Dermatology
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Quantitative characterization of antigens using monoclonal antibody reactivities

1993

A multipurpose program that empirically relates antigenic reactivities with monoclonal antibodies (MAbs) to genetic distances is presented. The program uses a set of known genetic pairwise distances to weigh each MAb depending on its capacity to define groups of taxonomically related antigens. This allows highly accurate identification and classification of unknown antigens. Also, the weights obtained constitute a quantitative measure of epitope conservation and can be used for improved vaccine design. © 1993 Oxford University Press.

Statistics and ProbabilityAnticorps monoclonalmedicine.drug_classComputational biologyMonoclonal antibodyBiochemistryEpitopeEpitopesAntigenMicrocomputersAntibodies monoclonalmedicineAntigensMolecular BiologyMathematicsbiologyAntibodies MonoclonalVirologyComputer Science ApplicationsQuantitative measureComputational MathematicsComputational Theory and Mathematicsbiology.proteinAntibodyAlgorithmsSoftware
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Antibodies directed to drug epitopes to investigate the structure of drug-protein photoadducts. Recognition of a common photobound substructure in ti…

2001

Drug-induced photoallergy is an immune adverse reaction to the combined effect of drugs and light. From the mechanistic point of view, it first involves covalent binding of drug to protein resulting in the formation of a photoantigen. Hence, determination of the structures of drug-protein photoadducts is of great relevance to understand the molecular basis of photoallergy and cross-immunoreactivity among drugs. Looking for new strategies to investigate the covalent photobinding of drugs to proteins, we generated highly specific antibodies to drug chemical substructures. The availability of such antibodies has allowed us to discriminate between the different modes by which tiaprofenic acid (…

StereochemistrySuprofenSuprofenPlasma protein bindingThiophenesToxicologyEpitopeAntibodieschemistry.chemical_compoundEpitopesStructure-Activity RelationshipThiophenemedicineMoietyStructure–activity relationshipAnimalsHumansDermatitis PhotoallergicAnti-Inflammatory Agents Non-SteroidalBenzeneGeneral MedicinechemistryCovalent bondKetoprofenAntibody FormationRabbitsPropionatesTiaprofenic acidmedicine.drugProtein BindingChemical research in toxicology
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Local control of antibody binding to hapten-presenting interfaces: Steric and electrostatic interaction

1991

The binding of labeled antibodies to hapten substituted monolayers at the air/water interface has been studied by means of fluorescence microscopy. Haptens with various spacer lengths between the epitope and a hydrocarbon chain, anchoring the molecule to the interface, have been synthesized. With DMPC,a unspecific binding has been shown to predominate over specific binding due to electrostatic interactions. At high surface pressures the bound antibody is detached because of steric interference with the lipid head groups. Due to a reduction of electrostatic interactions, no unspecific binding is observed to monolayers of cholesterol, which carries a small dipole moment. Mixed monolayers of c…

Steric effectsPolymers and PlasticsChemistryStereochemistryOrganic ChemistryCondensed Matter PhysicsElectrostaticsEpitopePhase (matter)MonolayerMaterials ChemistryBiophysicsFluorescence microscopeMoleculelipids (amino acids peptides and proteins)HaptenMakromolekulare Chemie. Macromolecular Symposia
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Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct f…

1994

The swine-specific coronavirus transmissible gastroenteritis virus (TGEV) uses pig aminopeptidase-N (pAPN) as a cellular receptor. We showed that the human aminopeptidase-N (hAPN) cannot substitute for pAPN in this respect, although the two enzymes have 80% amino acid sequence identity. In order to map the TGEV binding site on pAPN, we constructed a series of APN cDNA chimeras between pAPN and hAPN and analyzed them for their capacity to confer infectivity. The region between residues 717 and 813 was found to be essential for infectivity. This region also contains the epitopes for three TGEV-blocking monoclonal antibodies directed against pAPN. These data support the view that the catalytic…

SwineImmunologyMolecular Sequence DataBiologyCD13 Antigensmedicine.disease_causeVirus ReplicationMicrobiologyAminopeptidaseAminopeptidasesEpitopeVirusCatalysis03 medical and health sciencesSpecies SpecificityVirologymedicineVIRUS DE LA GASTROENTERITE TRANSMISSIBLEAnimalsHumansAmino Acid SequenceBinding siteCloning MolecularPeptide sequenceComputingMilieux_MISCELLANEOUS030304 developmental biologyCoronavirusInfectivity[SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology0303 health sciencesBinding SitesBase Sequence030302 biochemistry & molecular biologyTransmissible gastroenteritis virusVirology3. Good healthViral replicationMutagenesisInsect ScienceDNA Viral[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/VirologyReceptors VirusResearch Article
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Development of T cell clones reactive to two defined restriction elements in conjunction with two defined epitopes of antigen

1985

A previously described pig insulin (PI)-specific T cell line of (B10 X B10.BR)F1 origin was assayed for its reactivity with species variants of insulin in the presence of antigen-presenting cells (APC) of various H-2 haplotypes. In addition to its reactivity with PI and bovine insulin (BI) in the context of syngeneic F1 (H-2b X k)-APC, a weak cross-reactivity was observed with parental B10 (H-2b)-APC and BI but not PI. The cross-reactive cells could be selected out by several restimulations with the combination of BI and B10-APC. From the resulting, strongly cross-reactive T cell line several interleukin 2-dependent sublines were developed which did not require antigen-specific restimulatio…

SwineT-LymphocytesT cellImmunologyReceptors Antigen T-CellClone (cell biology)Context (language use)Cross ReactionsLymphocyte ActivationMajor histocompatibility complexEpitopeCell LineEpitopesMiceImmune systemAntigenmedicineAnimalsInsulinImmunology and AllergyGeneticsbiologyHistocompatibility Antigens Class IIT lymphocyteMolecular biologymedicine.anatomical_structurebiology.proteinInterleukin-2CattleEuropean Journal of Immunology
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Presentation of insulin and insulin A chain peptides to mouse T cells: involvement of cysteine residues.

1991

The requirements for insulin presentation and recognition by A alpha b A beta b- and A alpha b A beta k-restricted mouse T cells were studied using a variety of derivatives of the insulin A chain. It was found that A chain peptides with irreversibly blocked Cys residues are non-stimulatory for the T cells. This suggests that at least one of the Cys residues is essential for recognition. On the other hand, all A chain peptides containing Cys residues modified in a way reversible by reaction with thiols are stimulatory yet differ in antigenic potency. All these A chain derivatives including a 14 amino acid fragment require uptake by antigen presenting cells (APC) for efficient presentation. D…

Swinemedicine.medical_treatmentT-LymphocytesImmunologyAntigen presentationReceptors Antigen T-CellAntigen-Presenting CellsPeptideMice Inbred StrainsIn Vitro TechniquesCell LineEpitopesMiceAntigenmedicineAnimalsInsulinCysteineAntigen-presenting cellMolecular Biologychemistry.chemical_classificationChemistryInsulinT-cell receptorHistocompatibility Antigens Class IIChloroquineAmino acidBiochemistryCattleInterleukin-3PeptidesCysteineMolecular immunology
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Towards a fully synthetic MUC1-based anticancer vaccine: efficient conjugation of glycopeptides with mono-, di-, and tetravalent lipopeptides using c…

2011

Abstract The membrane-bound tumor-associated glycoprotein MUC1 is aberrantly glycosylated in cancer cells compared with normal cells, and is therefore considered an attractive target for cancer immunotherapy. However, tumor-associated glycopeptides from MUC1 do not elicit a sufficiently robust immune response. Therefore, antitumor vaccines were developed, which consist of MUC1 glycopeptides as the B epitopes and immune-stimulating toll-like receptor 2 (TLR 2) lipopeptide ligands. These fully synthetic vaccine candidates were prepared by solid-phase synthesis of the MUC1 glycopeptides. The Pam(3) Cys lipopeptide, also synthesized on solid-phase, was C-terminally coupled to oligovalent lysine…

Synthetic vaccineMagnetic Resonance SpectroscopyCarbohydrate chemistryMolecular Sequence DataAntineoplastic AgentsCancer VaccinesCatalysisEpitopeCell Linechemistry.chemical_compoundLipopeptidesMiceSolid-phase synthesisAnimalsHumansAntigens Tumor-Associated CarbohydrateVaccines SyntheticMembrane GlycoproteinsMolecular StructureOrganic ChemistryMucin-1GlycopeptidesLipopeptideGeneral ChemistryCombinatorial chemistryGlycopeptidechemistryClick chemistryClick ChemistryConjugateProtein BindingChemistry (Weinheim an der Bergstrasse, Germany)
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Water-Soluble Polymers Coupled with Glycopeptide Antigens and T-Cell Epitopes as Potential Antitumor Vaccines

2013

Highly decorated: Tumor-associated MUC1 glycopeptide and tetanus toxoid T-cell epitope P2 can be attached to water-soluble poly(N-(2-hydroxypropyl)methacrylamide) carriers by orthogonal ligation techniques. Fully synthetic vaccine A with additional nanostructure-promoting domains induced antibodies that exhibit high affinity to tumor cells.

Synthetic vaccineMolecular Sequence DataEpitopes T-LymphocyteCancer VaccinesCatalysisEpitopeMicechemistry.chemical_compoundPolymethacrylic AcidsAntigenAnimalsHumansMethacrylamideAmino Acid SequenceMUC1Vaccines SyntheticbiologyMucin-1GlycopeptidesToxoidWaterT-Lymphocytes Helper-InducerGeneral ChemistryMolecular biologyGlycopeptideSolubilityBiochemistrychemistryMCF-7 Cellsbiology.proteinAntibodyAngewandte Chemie International Edition
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