Search results for " Antibodies"

showing 10 items of 383 documents

Ubiquitin-like epitopes associated with Candida albicans cell surface receptors

1996

We have recently reported the cloning of a Candida albicans polyubiquitin gene and the presence of ubiquitin in the cell wall of this fungus. The polyubiquitin cDNA clone was isolated because of its reactivity with antibodies generated against the candidal 37-kDa laminin-binding protein. In the present study, we have further investigated the relationship between ubiquitin and cell wall components displaying receptor-like activities, including the 37-kDa laminin receptor, the 58-kDa fibrinogen-binding mannoprotein, and the candidal C3d receptor. Two-dimensional electrophoretic analysis and immunoblot experiments with antibodies against ubiquitin and the individually purified receptor-like mo…

GlycosylationImmunologyReceptors Cell SurfaceMicrobiologyEpitopeEpitopesUbiquitinCell surface receptorCandida albicansAnimalsCandida albicansReceptorUbiquitinsAntiserumbiologyImmune Serabiology.organism_classificationMolecular biologyCorpus albicansInfectious DiseasesBiochemistryPolyclonal antibodiesbiology.proteinParasitologyRabbitsResearch Article
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Immunochemical analysis of the carbohydrate moiety of yeast killer toxin K28

1990

Killer toxin K28, a 16 kd protein secreted by the wine yeast Saccharomyces cerevisiae strain 28, was reversibly bound by a column of Concanavalin A-Sepharose, confirming its glycoprotein nature. HPLC analysis of acid hydrolyzates of K28 toxin as well as Western-blots of beta-eliminated and/or endo H-treated killer toxin preparations probed with polyclonal alpha-toxin antibodies revealed that the carbohydrate moiety of K28 consists of D-mannose only, which is O-glycosidically linked via Ser/Thr residues to the protein part. The change in gel mobility of K28 after beta-elimination was caused by a decrease in molecular mass of about 1,800, corresponding to a carbohydrate moiety of 10 mannose r…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternSaccharomyces cerevisiaeMannoseSaccharomyces cerevisiaemedicine.disease_causeMicrobiologyChromatography Affinitychemistry.chemical_compoundmedicineMolecular BiologyAntibodies FungalChromatography High Pressure Liquidchemistry.chemical_classificationbiologyMolecular massToxinImmunochemistrySepharoseGeneral MedicineMycotoxinsbiology.organism_classificationKiller Factors YeastYeastchemistryBiochemistryPolyclonal antibodiesbiology.proteinGlycoproteinMannoseAntonie van Leeuwenhoek
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Cross-reactivity between tumor MHC class I-restricted antigens and an enterococcal bacteriophage

2020

International audience; Intestinal microbiota have been proposed to induce commensal-specific memory T cells that cross-react with tumor-associated antigens. We identified major histocompatibility complex (MHC) class I-binding epitopes in the tail length tape measure protein (TMP) of a prophage found in the genome of the bacteriophage Enterococcus hirae Mice bearing E. hirae harboring this prophage mounted a TMP-specific H-2Kb-restricted CD8+ T lymphocyte response upon immunotherapy with cyclophosphamide or anti-PD-1 antibodies. Administration of bacterial strains engineered to express the TMP epitope improved immunotherapy in mice. In renal and lung cancer patients, the presence of the ent…

H-2 AntigenProgrammed Cell Death 1 ReceptorCD8-Positive T-LymphocytesEpitopeEpitopesFecesMice0302 clinical medicineEnterococcus hiraeNeoplasmsMonoclonalBacteriophages0303 health sciencesMultidisciplinarybiologyAntibodies MonoclonalViral Tail ProteinsAlkylating3. Good healthmedicine.anatomical_structure030220 oncology & carcinogenesisCross ReactionEpitopeImmunotherapyHumanT cellAntineoplastic Agents[SDV.CAN]Life Sciences [q-bio]/CancerCross ReactionsMajor histocompatibility complexAntibodiesMicrobiology03 medical and health sciencesAnimals; Antibodies Monoclonal; Antigens Neoplasm; Antineoplastic Agents Alkylating; Bacteriophages; CD8-Positive T-Lymphocytes; Cross Reactions; Cyclophosphamide; Enterococcus hirae; Epitopes; Feces; Gastrointestinal Microbiome; H-2 Antigens; Histocompatibility Antigens Class I; Humans; Immunotherapy; Mice; Neoplasms; Programmed Cell Death 1 Receptor; Viral Tail Proteins[SDV.CAN] Life Sciences [q-bio]/CancerAntigenAntigens NeoplasmMHC class ImedicineAnimalsHumansAntigensBacteriophageAntineoplastic Agents AlkylatingCyclophosphamideProphage030304 developmental biologyEnterococcus hiraeAnimalHistocompatibility Antigens Class IH-2 AntigensCD8-Positive T-Lymphocytebiology.organism_classificationGastrointestinal Microbiomebiology.proteinNeoplasmFeceCD8
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HBV-specific immune defect in chronic hepatitis B (CHB) is correlated with a dysregulation of pro- and anti-inflammatory cytokines.

1999

SUMMARY The aim of this study was to examine the immunomodulating effects of rhIL-12 on the immune response induced by hepatitis B virus (HBV) antigens in clinical subgroups of patients with HBV infection. Peripheral blood mononuclear cells (PBMC) of 80 patients were stimulated with HBsAg, HBcAg, pre-S1Ag and tetanus toxoid in the absence or presence of IL-12 (0.01, 0.1 and 1 ng/ml). Stimulation by anti-CD3 + anti-CD28 and lipopolysaccharide (LPS) were used as controls. Proliferation and cytokine production were determined by 3H-thymidine uptake and ELISA after 72 h. After stimulation with HBV antigens only, production of tumour necrosis factor-alpha (TNF-α) or IL-10 was observed in all pat…

HBsAgHepatitis B virusImmunologyAntigen-Presenting CellsIn Vitro Techniquesmedicine.disease_causeLymphocyte ActivationHepatitis B AntigensInterferon-gammaHepatitis B ChronicOrthohepadnavirusmedicineImmunology and AllergyHumansHepatitis B AntibodiesHepatitisHepatitis B virusbiologybusiness.industryTumor Necrosis Factor-alphavirus diseasesOriginal ArticlesHepatitis Bmedicine.diseasebiology.organism_classificationVirologyInterleukin-12digestive system diseasesRecombinant ProteinsInterleukin-10HBcAgHBeAgHepadnaviridaeImmunologyDNA ViralLeukocytes MononuclearCytokinesInflammation MediatorsbusinessClinical and experimental immunology
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Rat and human liver cytosolic epoxide hydrolases: evidence for multiple forms at level of protein and mRNA.

1990

Two forms of human liver cytosolic epoxide hydrolase (cEH) with diagnostic substrate specificity for trans-stilbene oxide (cEHTSO) and cis-stilbene oxide (cEHCSO) have been identified, and cEHCSO was purified to apparent homogeneity. The enzyme had a monomer molecular weight of 49 kDa and an isoelectric point of 9.2. Pure cEHCSO hydrolyzed CSO at a rate of 145 nmole/min/mg. TSO was not metabolized at a detectable level, and like cEHTSO, the enzyme was about three times more active at pH 7.4 than at pH 9.0. Unlike cEHTSO, cEHCSO was efficiently inhibited by 1 mM 1-trichloropropene oxide (90.5%) and 1 mM STO (92%). Similarly, liver cEH purified 541-fold from fenofibrate induced Fischer 344 ra…

Health Toxicology and MutagenesisBiologyCytosolSpecies SpecificityWestern blotmedicineAnimalsHumansRNA MessengerEpoxide hydrolaseEpoxide Hydrolaseschemistry.chemical_classificationmedicine.diagnostic_testImmunochemistryPublic Health Environmental and Occupational HealthDNAMolecular biologyRatsMolecular WeightBlotIsoelectric pointEnzymeLiverBiochemistrychemistryPolyclonal antibodiesMicrosomal epoxide hydrolaseEpoxide Hydrolasesbiology.proteinResearch ArticleEnvironmental Health Perspectives
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Long-term efficacy of hepatitis B vaccine, booster policy, and impact of hepatitis B virus mutants

2005

The long-term efficacy of hepatitis B vaccine, long-term effectiveness of hepatitis B immunisation programmes, immune memory induced by hepatitis B vaccine, current booster policies, and impact of hepatitis B virus mutants on immunisation programmes were reviewed at the Viral Hepatitis Prevention Board (VHPB) meeting in Sevilla, Spain, March 2004. The main focus was on universal vaccination programmes with data being presented from Italy, Saudi Arabia, Singapore, Spain, Taiwan, Thailand, The Gambia, and USA (Alaska).

Hepatitis B vaccineSettore MED/42 - Igiene Generale e ApplicataImmunization Secondarymedicine.disease_causeTimeOrthohepadnavirusparasitic diseasesHumanshepatitis B vaccination long-term efficacy virus mutantsMedicineHepatitis B VaccinesHepatitis B AntibodiesHepatitis B virusGeneral VeterinaryGeneral Immunology and MicrobiologybiologyImmunization Programsbusiness.industryPublic Health Environmental and Occupational HealthHepatitis BHepatitis Bbiology.organism_classificationmedicine.diseaseVirologyVaccinationInfectious DiseasesHepadnaviridaeDNA ViralMutationMolecular MedicineViral diseasebusinessViral hepatitisImmunologic Memorygeographic locationsVaccine
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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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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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Mutation specific PCR and direct solid phase sequencing assay for the detection of hepatitis B virus pre-C/C mutants in anti-HBe-positive, chronic he…

1994

Sequence analysis of the HBV DNA from patients with anti-HBe+, chronic hepatitis B revealed that the lack of HBeAg is mostly due to a single GA transition at nucleotide position 1896, resulting in a translational stop codon. A point mutation-specific polymerase chain reaction (msPCR) for the detection of this genetic variant was established. Two serologically defined groups of patients with symptomatic chronic hepatitis B (HBeAg+ n = 14, anti-HBe+ n = 11) were included in this study. Viral DNA from 43 sera (26 eAg+/17 anti-HBe+) was amplified twice, using two different sets of PCR primers. Each set contained the same — strand primer, but the + strand primers differed at their 3′-end, thus b…

Hepatitis B virusHepatitis B virus DNA polymeraseMolecular Sequence DataBiologymedicine.disease_causePolymerase Chain Reactionlaw.inventionlawVirologymedicineHumansPoint MutationHepatitis B e AntigensHepatitis B AntibodiesPolymerase chain reactionDNA PrimersHepatitis B virusBase SequencePoint mutationvirus diseasesGenetic Variationbiology.organism_classificationHepatitis BVirologyMolecular biologydigestive system diseasesStop codonInfectious DiseasesHepadnaviridaeHBeAgDNA ViralPrimer (molecular biology)Journal of medical virology
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Biological standards for hepatitis B virus assays.

1992

Hepatitis B virusImmunoblottingBiologymedicine.disease_causePolymerase Chain ReactionVirusSerologylaw.inventionlawmedicineHumansHepatitis B AntibodiesPolymerase chain reactionHepatitis B virusHepatologyNucleic Acid HybridizationHepatitis BReference Standardsbiology.organism_classificationmedicine.diseaseHepatitis BVirologyIn vitroHepadnaviridaeDNA ViralViral diseaseJournal of hepatology
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