2001
Defective Antigen Processing in GILT-Free Mice
Maric M, Arunachalam B, Phan U, Dong C, Garrett W, Cannon K, Alfonso C, Karlsson L, Flavell R, Cresswell P. Defective Antigen Processing in GILT-Free Mice. Science 2001, 294: 1361-1365. PMID: 11701933, DOI: 10.1126/science.1065500.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsAntigen PresentationAntigen-Presenting CellsAntigensCell LineDendritic CellsDisulfidesEpitopesHistocompatibility Antigens Class IIHybridomasHydrogen-Ion ConcentrationImmunizationMiceMice, Inbred C57BLMice, KnockoutMolecular Sequence DataMuramidaseOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsProtein ConformationProtein FoldingSpleenT-LymphocytesCathepsin S Regulates the Expression of Cathepsin L and the Turnover of γ-Interferon-inducible Lysosomal Thiol Reductase in B Lymphocytes*
Honey K, Duff M, Beers C, Brissette W, Elliott E, Peters C, Maric M, Cresswell P, Rudensky A. Cathepsin S Regulates the Expression of Cathepsin L and the Turnover of γ-Interferon-inducible Lysosomal Thiol Reductase in B Lymphocytes*. Journal Of Biological Chemistry 2001, 276: 22573-22578. PMID: 11306582, DOI: 10.1074/jbc.m101851200.Peer-Reviewed Original ResearchConceptsB cellsCathepsin SMajor histocompatibility complex (MHC) class II moleculesClass II presentation pathwayT cell responsesPeripheral lymphoid organsCathepsin L proteinClass II moleculesInvariant chain cleavageAntigenic peptide fragmentsDendritic cellsLymphoid organsLysosomal thiol reductaseAntigen presentationPresentation pathwayB lymphocytesCell responsesMature giltsΓ-interferon-inducible lysosomal thiol reductaseInvariant chainThiol reductaseInducible lysosomal thiol reductaseNovel mechanismCathepsin LCells
1999
Thiol oxidation and reduction in MHC-restricted antigen processing and presentation
Cresswell P, Arunachalam B, Bangia N, Dick T, Diedrich G, Hughes E, Maric M. Thiol oxidation and reduction in MHC-restricted antigen processing and presentation. Immunologic Research 1999, 19: 191. PMID: 10493173, DOI: 10.1007/bf02786487.Peer-Reviewed Original Research
1998
The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules.
Hammond C, Denzin L, Pan M, Griffith J, Geuze H, Cresswell P. The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules. The Journal Of Immunology 1998, 161: 3282-91. PMID: 9759843, DOI: 10.4049/jimmunol.161.7.3282.Peer-Reviewed Original ResearchAssembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors.
Deng Y, Gibbs J, Bačík I, Porgador A, Copeman J, Lehner P, Ortmann B, Cresswell P, Bennink J, Yewdell J. Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors. The Journal Of Immunology 1998, 161: 1677-85. PMID: 9712031, DOI: 10.4049/jimmunol.161.4.1677.Peer-Reviewed Original ResearchMeSH KeywordsAedesAnimalsAntibodies, MonoclonalAntiportersCell LineEndoplasmic ReticulumH-2 AntigensHeLa CellsHumansImmunoglobulinsLymphocyte ActivationMacromolecular SubstancesMembrane Transport ProteinsMiceOligopeptidesOvalbuminPeptide FragmentsProtease InhibitorsRecombinant ProteinsT-LymphocytesVaccinia virusConceptsInsect cellsEndoplasmic reticulumVertebrate cellsHuman cellsHuman tapasinVaccinia virus-mediated expressionCell surface expressionProtease inhibitorsInefficient assemblyKbMHC class IMouse betaInsectsEfficient assemblyImmediate precursorSurface expressionAntigenic peptidesHeavy chainClass IRecombinant vaccinia virusVirus-mediated expressionAssemblyExpressionCellsVaccinia virusIntracellular formation and cell surface expression of a complex of an intact lysosomal protein and MHC class II molecules.
Arunachalam B, Pan M, Cresswell P. Intracellular formation and cell surface expression of a complex of an intact lysosomal protein and MHC class II molecules. The Journal Of Immunology 1998, 160: 5797-806. PMID: 9637490, DOI: 10.4049/jimmunol.160.12.5797.Peer-Reviewed Original ResearchAllelesAnimalsCell Transformation, ViralElectrophoresis, Polyacrylamide GelFlow CytometryFluorescent Antibody Technique, IndirectHerpesvirus 4, HumanHistocompatibility Antigens Class IIHLA-D AntigensHLA-DR AntigensLysosomesMiceOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsProteinsRabbitsSodium Dodecyl SulfateSurface PropertiesHLA-B27–Restricted Antigen Presentation in the Absence of Tapasin Reveals Polymorphism in Mechanisms of HLA Class I Peptide Loading
Peh C, Burrows S, Barnden M, Khanna R, Cresswell P, Moss D, McCluskey J. HLA-B27–Restricted Antigen Presentation in the Absence of Tapasin Reveals Polymorphism in Mechanisms of HLA Class I Peptide Loading. Immunity 1998, 8: 531-542. PMID: 9620674, DOI: 10.1016/s1074-7613(00)80558-0.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAnimalsAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersBeta 2-MicroglobulinCells, CulturedDisease SusceptibilityHLA-B AntigensHLA-B27 AntigenHLA-B44 AntigenHumansImmunoglobulinsMembrane Transport ProteinsMicePolymorphism, GeneticProtein BindingSurface PropertiesTransfectionProteases, processing, and thymic selection.
Cresswell P. Proteases, processing, and thymic selection. Science 1998, 280: 394-5. PMID: 9575085, DOI: 10.1126/science.280.5362.394.Peer-Reviewed Original ResearchCalnexin expression does not enhance the generation of MHC class I‐peptide complexes
Prasad S, Yewdell J, Porgador A, Sadasivan B, Cresswell P, Bennink J. Calnexin expression does not enhance the generation of MHC class I‐peptide complexes. European Journal Of Immunology 1998, 28: 907-913. PMID: 9541586, DOI: 10.1002/(sici)1521-4141(199803)28:03<907::aid-immu907>3.0.co;2-4.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, ViralATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBeta 2-MicroglobulinBiological TransportCalcium-Binding ProteinsCalnexinCell CompartmentationCells, CulturedH-2 AntigensHistocompatibility Antigens Class IHumansMacromolecular SubstancesMiceOvalbuminPeptidesProtein BindingGenomic analysis of the Tapasin gene, located close to the TAP loci in the MHC
Herberg J, Sgouros J, Jones T, Copeman J, Humphray S, Sheer D, Cresswell P, Beck S, Trowsdale J. Genomic analysis of the Tapasin gene, located close to the TAP loci in the MHC. European Journal Of Immunology 1998, 28: 459-467. PMID: 9521053, DOI: 10.1002/(sici)1521-4141(199802)28:02<459::aid-immu459>3.0.co;2-z.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBase SequenceCentromereExonsGenes, MHC Class IHistocompatibility Antigens Class IHumansImmunoglobulinsIntronsMembrane Transport ProteinsMiceMolecular Sequence DataPhylogenyRatsConceptsTapasin geneMouse ESTsSyntenic positionsGenomic analysisSeparate exonsGene sequencesDistinct phylogenyEndoplasmic reticulumGenesK locusChromosome 17IgC domainFunctional significanceLociMHC class IClass IHLA-DP locusTAP2 genesEquivalent locationsTAP transporterTapasin moleculePhylogenyIntronsChromosomesESTsQuantitative Defect in Staphylococcal Enterotoxin A Binding and Presentation by HLA-DM-Deficient T2.AkCells Corrected by Transfection of HLA-DM Genes
Albert L, Denzin L, Ghumman B, Bangia N, Cresswell P, Watts T. Quantitative Defect in Staphylococcal Enterotoxin A Binding and Presentation by HLA-DM-Deficient T2.AkCells Corrected by Transfection of HLA-DM Genes. Cellular Immunology 1998, 183: 42-51. PMID: 9578718, DOI: 10.1006/cimm.1997.1236.Peer-Reviewed Original Research
1996
HLA-DM Is Localized to Conventional and Unconventional MHC Class II–Containing Endocytic Compartments
Pierre P, Denzin L, Hammond C, Drake J, Amigorena S, Cresswell P, Mellman I. HLA-DM Is Localized to Conventional and Unconventional MHC Class II–Containing Endocytic Compartments. Immunity 1996, 4: 229-239. PMID: 8624813, DOI: 10.1016/s1074-7613(00)80431-8.Peer-Reviewed Original ResearchProcessing and delivery of peptides presented by MHC class I molecules
Lehner P, Cresswell P. Processing and delivery of peptides presented by MHC class I molecules. Current Opinion In Immunology 1996, 8: 59-67. PMID: 8729447, DOI: 10.1016/s0952-7915(96)80106-3.Peer-Reviewed Original ResearchAnimalsAntigen PresentationATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCysteine EndopeptidasesCytotoxicity, ImmunologicEndoplasmic ReticulumEpitopesHistocompatibility Antigens Class IHumansInterferon-gammaMiceMice, KnockoutModels, MolecularMultienzyme ComplexesProteasome Endopeptidase Complex
1995
HLA-DM induces clip dissociation from MHC class II αβ dimers and facilitates peptide loading
Denzin L, Cresswell P. HLA-DM induces clip dissociation from MHC class II αβ dimers and facilitates peptide loading. Cell 1995, 82: 155-165. PMID: 7606781, DOI: 10.1016/0092-8674(95)90061-6.Peer-Reviewed Original Research
1994
MHC class l/β2-microglobulin complexes associate with TAP transporters before peptide binding
Ortmann B, Androlewicz M, Cresswell P. MHC class l/β2-microglobulin complexes associate with TAP transporters before peptide binding. Nature 1994, 368: 864-867. PMID: 8159247, DOI: 10.1038/368864a0.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersB-LymphocytesBeta 2-MicroglobulinBiological TransportCalcium-Binding ProteinsCalnexinCarrier ProteinsCell LineDigitoninEndoplasmic ReticulumHistocompatibility Antigens Class IHLA-A3 AntigenHumansMiceMolecular Sequence DataProtein BindingRabbitsSolubility
1992
Chemistry and functional role of the invariant chain
Cresswell P. Chemistry and functional role of the invariant chain. Current Opinion In Immunology 1992, 4: 87-92. PMID: 1317713, DOI: 10.1016/0952-7915(92)90131-w.Peer-Reviewed Original Research
1990
The transport of class I major histocompatibility complex antigens is determined by sequences in the α1 and α2 protein domains
Alexander J, Payne J, Shigekawa B, Frelinger J, Cresswell P. The transport of class I major histocompatibility complex antigens is determined by sequences in the α1 and α2 protein domains. Immunogenetics 1990, 31: 169-178. PMID: 2318516, DOI: 10.1007/bf00211552.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsAntigens, SurfaceBiological TransportCell LineElectricityElectrophoresis, Gel, Two-DimensionalExonsFlow CytometryGlycosylationHistocompatibility Antigens Class IHLA-B7 AntigenHumansMiceMolecular Sequence DataProtein ConformationProtein Processing, Post-TranslationalRecombinant ProteinsT-LymphocytesTransfectionQuestions of presentation
Cresswell P. Questions of presentation. Nature 1990, 343: 593-594. PMID: 2304528, DOI: 10.1038/343593a0.Peer-Reviewed Original Research
1989
Differential transport requirements of HLA and H-2 class I glycoproteins
Alexander J, Payne J, Murray R, Frelinger J, Cresswell P. Differential transport requirements of HLA and H-2 class I glycoproteins. Immunogenetics 1989, 29: 380-388. PMID: 2731965, DOI: 10.1007/bf00375866.Peer-Reviewed Original Research
1987
Immune recognition of human major histocompatibility antigens: localization by a comprehensive synthetic strategy of the continuous antigenic sites in the first domain of HLA‐DR2 β chain
Ulrich R, Atassi H, Lutz P, Cresswell P, Atassi M. Immune recognition of human major histocompatibility antigens: localization by a comprehensive synthetic strategy of the continuous antigenic sites in the first domain of HLA‐DR2 β chain. European Journal Of Immunology 1987, 17: 497-502. PMID: 2436923, DOI: 10.1002/eji.1830170410.Peer-Reviewed Original ResearchConceptsAntibody-binding activityHuman major histocompatibility antigensBeta chainMajor histocompatibility antigensAntigenic sitesHistocompatibility antigensImmune recognitionChain antiserumIsolated beta chainsMost antiseraAntiserumPeptide 81Continuous antigenic sitesΒ-chainPeptidesFirst domainHLAImmunodominanceAntigenComprehensive synthetic strategy