Search results for "Antigen processing"

showing 10 items of 71 documents

Cathepsin B in Antigen-Presenting Cells Controls Mediators of the Th1 Immune Response during Leishmania major Infection

2014

Resistance and susceptibility to Leishmania major infection in the murine model is determined by the capacity of the host to mount either a protective Th1 response or a Th2 response associated with disease progression. Previous reports involving the use of cysteine cathepsin inhibitors indicated that cathepsins B (Ctsb) and L (Ctsl) play important roles in Th1/Th2 polarization during L. major infection in both susceptible and resistant mouse strains. Although it was hypothesized that these effects are a consequence of differential patterns of antigen processing, the mechanisms underlying these differences were not further investigated. Given the pivotal roles that dendritic cells and macrop…

Cathepsin Lmedicine.medical_treatmentCathepsin BCathepsin BWhite Blood CellsMiceAnimal CellsMedicine and Health SciencesLeishmaniasisLeishmania majorProtozoansAntigen PresentationMice Inbred BALB CT CellsAntigen processinglcsh:Public aspects of medicineInterleukin-12Up-RegulationInfectious DiseasesCytokineInterleukin 12FemaleCellular TypesResearch ArticleNeglected Tropical Diseaseslcsh:Arctic medicine. Tropical medicinelcsh:RC955-962Immune CellsImmunologyAntigen presentationAntigen-Presenting CellsMice TransgenicBiologyMajor histocompatibility complexmedicineAnimalsAntigen-presenting cellMHC class IIBlood CellsMacrophagesOrganismsPublic Health Environmental and Occupational HealthBiology and Life Scienceslcsh:RA1-1270Cell BiologyDendritic CellsTh1 CellsTropical DiseasesMolecular biologyParasitic ProtozoansDisease Models AnimalImmunologybiology.proteinPLoS Neglected Tropical Diseases
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Immune evasion proteins of murine cytomegalovirus preferentially affect cell surface display of recently generated peptide presentation complexes.

2009

CD8 T cells recognize infected cells by interaction of their T-cell receptor (TCR) with a cell surface presentation complex composed of a cognate antigenic peptide bound to a presenting allelic form of a major histocompatibility complex class I (MHC-I) glycoprotein (77, 85, 97, 98). The number of such “peptide receptors” per cell has been estimated to be on the order of 105 to 106 for each MHC-I allomorph (for a review, see reference 82). Viral antigenic peptides are generated within infected cells by proteolytic processing of viral proteins, usually in the proteasome, and associate with nascent MHC-I proteins in the endoplasmic reticulum (ER) before the peptide-MHC (pMHC) complexes travel …

Chromosomes Artificial BacterialMuromegalovirusImmunologyAntigen presentationchemical and pharmacologic phenomenaBiologyMajor histocompatibility complexMicrobiologyEpitopeMiceViral ProteinsAntigenVirologyCytotoxic T cellAnimalsCells CulturedDNA PrimersImmune EvasionBase SequenceAntigen processingT-cell receptorHistocompatibility Antigens Class IVirologyMice Inbred C57BLMutagenesisInsect Sciencebiology.proteinPathogenesis and ImmunityPeptidesCD8Journal of virology
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The efficient bovine insulin presentation capacity of bone marrow-derived macrophages activated by granulocyte-macrophage colony-stimulating factor c…

1993

Bone marrow-derived macrophages (BMM phi) were shown before to function as antigen-presenting cells. We show here, that the antigen presentation capacity of BMM phi depends on the nature of the antigen and is differently regulated by the lymphokines interferon-gamma (IFN-gamma) and granulocyte/macrophage-colony-stimulating factor (GM-CSF). When bovine insulin (BI) was employed as antigen, only BMM phi treated with GM-CSF (GM-CSF-M phi) were efficient presenters, but when presentation of the antigens ovalbumin and conalbumin was tested, IFN-gamma-pulsed BMM phi (IFN-gamma-M phi) proved superior to GM-CSF-M phi. The lack of efficient BI presentation function of IFN-gamma-M phi was only obviou…

CytoplasmImmunologyAntigen presentationAntigen-Presenting CellsBone Marrow CellsBiologyInterferon-gammachemistry.chemical_compoundAntigenmedicineAnimalsInsulinImmunology and AllergyCysteineSulfhydryl CompoundsAntigen-presenting cellAntigen processingMacrophagesLymphokineGranulocyte-Macrophage Colony-Stimulating FactorGlutathioneMacrophage ActivationGlutathioneCell biologyGranulocyte macrophage colony-stimulating factorBiochemistrychemistryCattleIntracellularmedicine.drugEuropean Journal of Immunology
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Impaired Transporter Associated with Antigen Processing (TAP) Function Attributable to a Single Amino Acid Alteration in the Peptide TAP Subunit TAP1

2003

Abstract The heterodimeric peptide transporter TAP belongs to the ABC transporter family. Sequence comparisons with the P-glycoprotein and cystic fibrosis transmembrane conductance regulator and the functional properties of selective amino acids in these ABC transporters postulated that the glutamic acid at position 263 and the phenylalanine at position 265 of the TAP1 subunit could affect peptide transporter function. To define the role of both amino acids, TAP1 mutants containing a deletion or a substitution to alanine at position 263 or 265 were generated and stably expressed in murine and human TAP1−/− cells. The different TAP1 mutants were characterized in terms of expression and funct…

Cytotoxicity ImmunologicMacromolecular SubstancesPhenylalanineImmunologyAntigen presentationGlutamic AcidATP-binding cassette transporterEndoplasmic ReticulumTransfectionCell LineMiceAdenosine TriphosphateATP Binding Cassette Transporter Subfamily B Member 3MHC class IAnimalsHumansImmunology and AllergyATP Binding Cassette Transporter Subfamily B Member 2Sequence DeletionAlaninechemistry.chemical_classificationAntigen PresentationbiologyHistocompatibility Antigens Class I3T3 CellsIntracellular MembranesTransporter associated with antigen processingMolecular biologyPeptide FragmentsCystic fibrosis transmembrane conductance regulatorAmino acidMice Inbred C57BLProtein SubunitsAmino Acid SubstitutionBiochemistrychemistryMutagenesis Site-Directedbiology.proteinATP-Binding Cassette TransportersTAP1Sequence AlignmentProtein BindingT-Lymphocytes CytotoxicThe Journal of Immunology
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Impact of antigen presentation on TCR modulation and cytokine release: implications for detection and sorting of antigen-specific CD8+ T cells using …

2002

Abstract Soluble MHC class I molecules loaded with antigenic peptides are available either to detect and to enumerate or, alternatively, to sort and expand MHC class I-restricted and peptide-reactive T cells. A defined number of MHC class I/peptide complexes can now be implemented to measure T cell responses induced upon Ag-specific stimulation, including CD3/CD8/ζ-chain down-regulation, pattern, and quantity of cytokine secretion. As a paradigm, we analyzed the reactivity of a Melan-A/MART-1-specific and HLA-A2-restricted CD8+ T cell clone to either soluble or solid-phase presented peptides, including the naturally processed and presented Melan-A/MART-1 peptide AAGIGILTV or the peptide ana…

Cytotoxicity ImmunologicT cellCD8 AntigensImmunologyAntigen presentationReceptors Antigen T-CellDown-RegulationEpitopes T-LymphocyteCD8-Positive T-LymphocytesMHC class IHLA-A2 AntigenmedicineImmunology and AllergyCytotoxic T cellHumansAntigen PresentationPeptide analogbiologyAntigen processingMembrane ProteinsMHC restrictionMolecular biologymedicine.anatomical_structureAmino Acid SubstitutionReceptor-CD3 Complex Antigen T-Cellbiology.proteinMutagenesis Site-DirectedCytokinesCD8Journal of immunology (Baltimore, Md. : 1950)
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Enhanced susceptibility to cytotoxic T lymphocytes without increase of MHC class I antigen expression after conditional overexpression of heat shock …

1999

Antigenic peptides have been found associated with heat shock proteins (HSP) including cytoplasmic HSP70 and heat shock cognate protein 70 as well as the endoplasmic reticulum-resident glucose-regulated protein 94. Recently, HSP70 transfection has been reported to increase MHC class I cell surface expression and antigen presentation on mouse melanoma B16 cells (Wells et al., Int. Immunol. 1998. 10: 609). To analyze the effect of HSP70 on MHC class I cell surface expression and lysability of target cells we transfected a human melanoma cell line with the rat Hsp70-1 gene using the Tet-On system for conditional overexpression of HSP70. Induction of HSP70 did not increase cell surface expressi…

Cytotoxicity ImmunologicT-LymphocytesImmunologyAntigen presentationCD1BiologyMajor histocompatibility complexMajor Histocompatibility ComplexMiceMHC class ITumor Cells CulturedImmunology and AllergyCytotoxic T cellAnimalsHumansHSP70 Heat-Shock ProteinsMelanomaAntigen PresentationAntigen processingMHC class I antigenGene Transfer TechniquesMHC restrictionMolecular biologyRatsGene Expression Regulation Neoplasticbiology.proteinEuropean journal of immunology
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The sequence alteration associated with a mutational hotspot in p53 protects cells from lysis by cytotoxic T lymphocytes specific for a flanking pept…

1998

A high proportion of tumors arise due to mutation of the p53 tumor suppressor protein. A p53 hotspot mutation at amino acid position 273 from R to H, flanking a peptide epitope that spans residues 264–272, renders cells resistant to killing by human histocompatibility leukocyte antigen (HLA)-A*0201–restricted cytotoxic T lymphocytes (CTLs) specific for this epitope. Acquisition of the R to H mutation at residue 273 of the human p53 protein promotes tumor growth in vivo by selective escape from recognition by p53.264–272 peptide-specific CTLs. Synthetic 27-mer p53 polypeptides covering the antigenic nonamer region 264–272 of p53 were used as proteasome substrates to investigate whether the R…

Cytotoxicity Immunologicp53Epitopes T-LymphocyteEpitopeSubstrate SpecificityMice0302 clinical medicineTumor Cells CulturedImmunology and AllergyCytotoxic T cellPeptide sequence0303 health sciencesAntigen PresentationproteasomesHydrolysisArticles3. Good healthCysteine Endopeptidasestumor antigensCell DivisionProteasome Endopeptidase ComplexImmunologyAntigen presentationMolecular Sequence DataMice TransgenicBiologyArgininecytotoxic T lymphocytes03 medical and health sciencesAntigenMultienzyme Complexesantigen processingAnimalsHumansPoint MutationHistidineAmino Acid Sequence030304 developmental biologyBinding SitesLinear epitopeHLA-A AntigensPoint mutationCytotoxicity Tests ImmunologicMolecular biologyPeptide FragmentsCTL*Tumor Suppressor Protein p53Peptides030215 immunologyT-Lymphocytes CytotoxicThe Journal of experimental medicine
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Purification of Large Cytosolic Proteases for In Vitro Assays: 20S and 26S Proteasomes

2012

Proteasomes are the main cytosolic proteases responsible for generating peptides for antigen processing and presentation in the MHC (major histocompatibility complex) class-I pathway. Purified 20S and 26S proteasomes have been widely used to study both specificity and efficiency of antigen processing. Here, we describe the purification of active human 20S and 26S proteasomes from human erythrocytes by DEAE-ion exchange chromatography, ammonium sulfate precipitation, glycerol density gradient centrifugation, and Superose-6 size exclusion chromatography and their characterization using fluorogenic substrates and specific inhibitors.

Differential centrifugationCytosolProteasesProteasomebiologyBiochemistryAntigen processingChemistrybiology.proteinMajor histocompatibility complexPolyacrylamide gel electrophoresisAmmonium sulfate precipitation
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Human cytomegalovirus US3 modulates destruction of MHC class I molecules

2012

Human cytomegalovirus (HCMV), a member of the Herpesviridae family, is proficient at establishing lifelong persistence within the host in part due to immune modulating genes that limit immune recognition. HCMV encodes at least five glycoproteins within its unique short (US) genomic region that interfere with MHC class I antigen presentation, thus hindering viral clearance by cytotoxic T lymphocytes (CTL). Specifically, US3 retains class I within the endoplasmic reticulum (ER), while US2 and US11 induce class I heavy chain destruction. A cooperative effect on class I down-regulation during stable expression of HCMV US2 and US3 has been established. To address the impact of US3 on US11-mediat…

Genes ViralAntigen processingMHC class I antigenvirusesHistocompatibility Antigens Class IImmunologyAntigen presentationCD1CytomegalovirusFluorescent Antibody TechniqueTransporter associated with antigen processingBiologyMajor histocompatibility complexVirologyArticleCell LineViral ProteinsMHC class Ibiology.proteinHumansCytotoxic T cellMolecular BiologyMolecular Immunology
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Identification of sequences in the human peptide transporter subunit TAP1 required for transporter associated with antigen processing (TAP) function

2001

The heterodimeric peptide transporter associated with antigen processing (TAP) consisting of the subunits TAP1 and TAP2 mediates the transport of cytosolic peptides into the lumen of the endoplasmic reticulum (ER). In order to accurately define domains required for peptide transporter function, a molecular approach based on the construction of a panel of human TAP1 mutants and their expression in TAP1(-/-) cells was employed. The characteristics and biological activity of the various TAP1 mutants were determined, and compared to that of wild-type TAP1 and TAP1(-/-) control cells. All mutant TAP1 proteins were localized in the ER and were capable of forming complexes with the TAP2 subunit. H…

Genetic VectorsImmunologyAntigen presentationBiological Transport ActiveEpitopes T-LymphocyteTransfectionMajor histocompatibility complexMiceAntigenATP Binding Cassette Transporter Subfamily B Member 3MHC class ITumor Cells CulturedAnimalsHumansLymphocytic choriomeningitis virusImmunology and AllergyAmino Acid SequenceATP Binding Cassette Transporter Subfamily B Member 2Sequence DeletionMice KnockoutAntigen PresentationbiologyAntigen processingHistocompatibility Antigens Class IGeneral MedicineTransporter associated with antigen processingMHC restrictionCytotoxicity Tests ImmunologicMolecular biologyPeptide FragmentsCell biologyMice Inbred C57BLPeptide transportMutagenesis Site-Directedbiology.proteinATP-Binding Cassette TransportersDimerizationT-Lymphocytes CytotoxicInternational Immunology
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