Search results for "epitope"

showing 10 items of 455 documents

Reduced hepatitis B virus surface antigen-specific Th1 helper cell frequency of chronic HBV carriers is associated with a failure to produce antigen-…

2000

In chronic hepatitis B virus (HBV) infection weak antiviral immune responses are associated with viral persistence. We studied possible immune deficits underlying the lack of serum antibodies of such patients against the HBV surface antigen (HBsAg) in a novel human/mouse chimeric model. A hepatitis B surface antigen (HBs) vaccination of Balb/c mice engrafted with peripheral blood mononuclear cells (PBMC) of naturally HBV-immunized donors induced high frequencies of human HBsAg-specific B and T helper 1 (Th1) cells. These responses were associated with high serum anti-HBs antibody levels of the subclasses immunoglobulin G1 (IgG1) and IgG2 that are driven by interleukin-2 (IL-2) and interfero…

HBsAgHepatologyvirus diseasesViremiaBiologyHepatitis Bmedicine.diseaseVirologydigestive system diseasesEpitopeVirusImmune systemAntigenImmunologymedicinebiology.proteinAntibodyHepatology
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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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A catalog of HLA type, HLA expression, and neo-epitope candidates in human cancer cell lines

2014

Cancer cell lines are a tremendous resource for cancer biology and therapy development. These multipurpose tools are commonly used to examine the genetic origin of cancers, to identify potential novel tumor targets, such as tumor antigens for vaccine devel-opment, and utilized to screen potential therapies in preclinical studies. Mutations, gene expression, and drug sensitivity have been determined for many cell lines using next-generation sequencing (NGS). However, the human leukocyte antigen (HLA) type and HLA expression of tumor cell lines, characterizations necessary for the development of cancer vaccines, have remained largely incomplete and, such information, when available, has been …

HLA typeCCLE Cancer Cell Line Encyclopediamedicine.medical_treatmentCOSMIC Catalog of Somatic Mutations in CancerImmunologyBRENDA BRaunschweig ENzyme DatabaseSNV single nucleotide variationRNA-SeqHuman leukocyte antigenBiologynsSNV non synonymous SNVTranscriptomeLoss of heterozygosityAntigenGenotypemedicineImmunology and AllergyRNA-SeqRNA-Seq RNA SequencingOriginal ResearchGeneticsHLA expressionneoepitopescancer cell linesSRA Sequence Read ArchiveCancerImmunotherapymedicine.diseaseHLA Human Leukocyte AntigenOncologyRPKM reads per kilobase of exon model per million mapped readsIEDB Immune Epitope Databasesomatic mutationsimmunotherapyDLBCL diffuse large B-cell lymphomaNGS Next Generation SequencingOncoImmunology
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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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Behavior of a Short preS1 Epitope on the Surface of Hepatitis B Core Particles

1999

The major immunodominant region of hepatitis B core particles is widely recognized as the most prospective target for the insertion of foreign epitopes, ensuring their maximal antigenicity and immunogenicity. This region was mapped around amino acid residues 79-81, which were shown by electron cryo-microscopy to be located on the tips of the spikes protruding from the surface of hepatitis B core shells. Here we tried to expose a model sequence, the short immunodominant hepatitis B preS1 epitope 31-DPAFR-35, onto the tip of the spike, with simultaneous deletion of varying stretches from the major immunodominant region of the HBc molecule. Accessibility to the monoclonal anti-preS1 antibody M…

Hepatitis B virusAntigenicityRecombinant Fusion ProteinsGenetic VectorsMolecular Sequence DataClinical BiochemistryAntigen presentationmedicine.disease_causeBiochemistryEpitopeMicemedicineAnimalsHumansAmino Acid SequenceProtein PrecursorsMolecular BiologyPeptide sequenceHepatitis B virusAntigen PresentationMice Inbred BALB CHepatitis B Surface AntigensbiologyImmunodominant EpitopesChemistryImmunogenicityHepatitis B Core AntigensVirologyPolyclonal antibodiesbiology.proteinEpitopes B-LymphocyteFemaleRabbitsAntibodyPlasmidsBiological Chemistry
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Interaction of wild-type and naturally occurring deleted variants of hepatitis B virus core polypeptides leads to formation of mosaic particles

2000

AbstractThe simultaneous presence of hepatitis B virus (HBV) genomes carrying wild-type (wt) and in-frame deleted variants of the HBV core gene has been identified as a typical feature of HBV-infected renal transplant patients with severe liver disease. To investigate possible interactions of wt and deleted core polypeptides a two-vector Escherichia coli expression system ensuring their concomitant synthesis has been developed. Co-expression of wt and a mutant core lacking 17 amino acid residues (77–93) within the immunodominant region led to the formation of mosaic particles, whereas the mutant alone was incapable of self-assembly.

Hepatitis B virusBlotting WesternMutantBiophysicsBiologymedicine.disease_causeBiochemistryGenomeHepatitis B virus PRE betaLiver diseaseStructural BiologyEscherichia coliGeneticsmedicineProtein Structure QuaternaryMolecular BiologyEscherichia coliSequence DeletionHepatitis B virusImmunodominant EpitopesHepatitis B virus coreViral Core ProteinsVirus AssemblyWild typeGenetic VariationCell Biologymedicine.diseaseDimer formationHepatitis B Core AntigensPrecipitin TestsVirologyMolecular biologyRecombinant ProteinsMosaic particleMicroscopy ElectronPeptidesDimerizationC gene deletionProtein BindingFEBS Letters
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Hepatitis B core particles as a universal display model: a structure-function basis for development

1999

AbstractBecause it exhibits a remarkable capability to accept mutational intervention and undergo correct folding and self-assembly in all viable prokaryotic and eukaryotic expression systems, hepatitis B core (HBc) protein has been favored over other proposed particulate carriers. Structurally, the unusual α-helical organization of HBc dimeric units allows introduction of foreign peptide sequences into several areas of HBc shells, including their most protruding spikes. Progress toward full resolution of the spatial structure as well as accumulation of chimeric HBc-based structures has brought closer the knowledge-based design of future vaccines, gene therapy tools and other artificial par…

Hepatitis B virusGenes ViralCryo-electron microscopyMacromolecular SubstancesProtein ConformationBiophysicsComputational biologyBiologyBiochemistryMolecular displayEpitopesProtein structureStructural BiologyGeneticsProkaryotic expressionAnimalsHumansMolecular BiologyDrug CarriersBinding SitesSpatial structureViral Core ProteinsStructure functionHepatitis B core proteinvirus diseasesCell BiologyBasis (universal algebra)Self-assemblyAntigenicityVirologyBiological EvolutionHepatitis B Core Antigensdigestive system diseasesFolding (chemistry)Protein structureElectron cryomicroscopyDimerizationHepatitis b coreFEBS Letters
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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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Stop codon insertion restores the particle formation ability of hepatitis B virus core-hantavirus nucleocapsid protein fusions.

2003

In recent years, epitopes of various origin have been inserted into the core protein of hepatitis B virus (HBc), allowing the formation of chimeric HBc particles. Although the C-terminus of a C-terminally truncated HBc (HBcΔ) tolerates the insertion of extended foreign sequences, the insertion capacity is still a limiting factor for the construction of multivalent vaccines. Previously, we described a new system to generate HBcΔ mosaic particles based on a read-through mechanism in an <i>Escherichia coli</i> suppressor strain [J Gen Virol 1997;78:2049–2053]. Those mosaic particles allowed the insertion of a 114-amino acid (aa)-long segment of a Puumala hantavirus (PUUV) nucleocap…

Hepatitis B virusHepatitis B virus DNA polymerasevirusesRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeEpitopeHepatitis B virus PRE betaMiceVirologyparasitic diseasesmedicineAnimalsNucleocapsidHantavirusHepatitis B virusMice Inbred BALB CBase SequenceChemistryHepatitis B virus coreVirionvirus diseasesNucleocapsid ProteinsVirologyMolecular biologyHepatitis B Core Antigensdigestive system diseasesStop codonNS2-3 proteaseInfectious DiseasesCodon TerminatorImmunizationIntervirology
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Selection of hepatitis B virus variants with aminoacid substitutions inside the core antigen during interferon-? therapy

2000

The hepatitis B virus (HBV) core antigen carries many epitopes relevant for B and T cell response that show aminoacid variation during viral infection. In a longitudinal analysis, sequential serum samples of 15 patients that suffered from chronic HBV infection were collected before, during, and after high-dose IFN-α treatment. The HBV preCore/Core (preC/C) sequence of the selected samples in each patient was determined and analysed for sequence variations compared to the pretreatment sample. The positions of HBV core aminoacid substitutions were assigned to immunodominant B, CD4+ and CD8+ cell epitopes. Seventy-five percent of all aminoacid substitutions were found within immunodominant T a…

Hepatitis B virusbiologyAlpha interferonmedicine.disease_causebiology.organism_classificationVirologyEpitopeVirusInfectious DiseasesAntigenOrthohepadnavirusHepadnaviridaeVirologymedicineAntigenic variationJournal of Medical Virology
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