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-LymphocytesDistinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP)
Karttunen J, Lehner P, Gupta S, Hewitt E, Cresswell P. Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP). Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 7431-7436. PMID: 11381133, PMCID: PMC34686, DOI: 10.1073/pnas.121180198.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SubstitutionAnimalsATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersAzidesBinding SitesCell LineHeLa CellsHumansLysineMajor Histocompatibility ComplexMutagenesis, Site-DirectedPeptide FragmentsPhotoaffinity LabelsProtein SubunitsRecombinant ProteinsTransfection
2000
Gamma-Interferon-inducibleLysosomal Thiol Reductase (GILT) MATURATION, ACTIVITY, AND MECHANISM OF ACTION*
Phan U, Arunachalam B, Cresswell P. Gamma-Interferon-inducibleLysosomal Thiol Reductase (GILT) MATURATION, ACTIVITY, AND MECHANISM OF ACTION*. Journal Of Biological Chemistry 2000, 275: 25907-25914. PMID: 10852914, DOI: 10.1074/jbc.m003459200.Peer-Reviewed Original Research
1999
The N‐terminal region of tapasin is required to stabilize the MHC class I loading complex
Bangia N, Lehner P, Hughes E, Surman M, Cresswell P. The N‐terminal region of tapasin is required to stabilize the MHC class I loading complex. European Journal Of Immunology 1999, 29: 1858-1870. PMID: 10382748, DOI: 10.1002/(sici)1521-4141(199906)29:06<1858::aid-immu1858>3.0.co;2-c.Peer-Reviewed Original ResearchAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBase SequenceBeta 2-MicroglobulinBinding SitesBiological Transport, ActiveCalcium-Binding ProteinsCalreticulinCell LineDNA PrimersDrug StabilityHeat-Shock ProteinsHistocompatibility Antigens Class IHumansImmunoglobulinsIsomerasesKineticsMacromolecular SubstancesMembrane Transport ProteinsMolecular ChaperonesProtein BindingProtein Disulfide-IsomerasesRibonucleoproteins
1998
Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene
Copeman J, Bangia N, Cross J, Cresswell P. Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene. European Journal Of Immunology 1998, 28: 3783-3791. PMID: 9842921, DOI: 10.1002/(sici)1521-4141(199811)28:11<3783::aid-immu3783>3.0.co;2-9.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersB-LymphocytesCell LineDNA, ComplementaryEndoplasmic ReticulumExonsHumansImmunoglobulinsMembrane Transport ProteinsMutationPolymorphism, GeneticReverse Transcriptase Polymerase Chain ReactionConceptsMutant cell linesEndoplasmic reticulumAlternative splicingN-terminal 49 amino acidsGenetic basisTapasin geneExon twoWild-type cellsFull-length transcriptsCell linesSingle nucleotide substitutionSignal peptideSecond intronNucleotide substitutionsPhysical associationSplice siteGlycoprotein tapasinPosition 240Amino acidsClass I moleculesSplicingOptimal bindingGenesI moleculesHeterodimersAssembly 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 virus
1997
Regulation of MHC class I heterodimer stability and interaction with TAP by tapasin
Grandea III A, Lehner PJ, Cresswell P, Spies T. Regulation of MHC class I heterodimer stability and interaction with TAP by tapasin. Immunogenetics 1997, 46: 477-483. PMID: 9321427, DOI: 10.1007/s002510050308.Peer-Reviewed Original ResearchUltraviolet B irradiation reduces the surface expression of conformationally correct class I and II histocompatibility antigens
Tambur A, Foster P, Mellins E, Cresswell P, Faustman D, Gebel H. Ultraviolet B irradiation reduces the surface expression of conformationally correct class I and II histocompatibility antigens. Transplantation Proceedings 1997, 29: 2689-2691. PMID: 9290791, DOI: 10.1016/s0041-1345(97)00557-5.Peer-Reviewed Original ResearchA Critical Role for Tapasin in the Assembly and Function of Multimeric MHC Class I-TAP Complexes
Ortmann B, Copeman J, Lehner P, Sadasivan B, Herberg J, Grandea A, Riddell S, Tampé R, Spies T, Trowsdale J, Cresswell P. A Critical Role for Tapasin in the Assembly and Function of Multimeric MHC Class I-TAP Complexes. Science 1997, 277: 1306-1309. PMID: 9271576, DOI: 10.1126/science.277.5330.1306.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCalcium-Binding ProteinsCalreticulinCell LineCell Line, TransformedChromosome MappingChromosomes, Human, Pair 6Cloning, MolecularDimerizationEndoplasmic ReticulumGenetic LinkageHistocompatibility Antigens Class IHLA AntigensHumansImmunoglobulin GImmunoglobulinsMajor Histocompatibility ComplexMembrane Transport ProteinsMolecular Sequence DataRibonucleoproteinsSequence Homology, Amino AcidT-Lymphocytes, CytotoxicTumor Cells, Cultured
1996
Trimeric Interactions of the Invariant Chain and Its Association with Major Histocompatibility Complex Class II αβ Dimers*
Newcomb J, Carboy-Newcomb C, Cresswell P. Trimeric Interactions of the Invariant Chain and Its Association with Major Histocompatibility Complex Class II αβ Dimers*. Journal Of Biological Chemistry 1996, 271: 24249-24256. PMID: 8798670, DOI: 10.1074/jbc.271.39.24249.Peer-Reviewed Original ResearchRoles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP
Sadasivan B, Lehner P, Ortmann B, Spies T, Cresswell P. Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP. Immunity 1996, 5: 103-114. PMID: 8769474, DOI: 10.1016/s1074-7613(00)80487-2.Peer-Reviewed Original ResearchATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBeta 2-MicroglobulinCalcium-Binding ProteinsCalreticulinCell LineGlycoproteinsHistocompatibility Antigens Class IHLA-A AntigensHLA-B AntigensHLA-C AntigensHumansIndolizinesMolecular ChaperonesMutationPeptidesRibonucleoproteinsHLA-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 ResearchClass I-like CD1A-C Do Not Protect Target Cells from NK-Mediated Cytolysis
Storkus W, Wei M, Cresswell P, Dawson J. Class I-like CD1A-C Do Not Protect Target Cells from NK-Mediated Cytolysis. Cellular Immunology 1996, 167: 154-156. PMID: 8548840, DOI: 10.1006/cimm.1996.0020.Peer-Reviewed Original ResearchConceptsClass INatural killer cell-mediated cytolysisTarget cellsCell-mediated cytolysisTarget cell susceptibilityNonclassical MHC class IHLA class ITarget cell sensitivityMHC class INatural killingNK cellsCD1c moleculesElevated expressionCell susceptibilityCell sensitivityCD1aCytolysisNKClonal transfectantsRelevant levelsCellsCell surfaceLysisPrevious studiesCD1b
1995
Assembly, Intracellular Localization, and Nucleotide Binding Properties of the Human Peptide Transporters TAP1 and TAP2 Expressed by Recombinant Vaccinia Viruses (∗)
Russ G, Esquivel F, Yewdell J, Cresswell P, Spies T, Bennink J. Assembly, Intracellular Localization, and Nucleotide Binding Properties of the Human Peptide Transporters TAP1 and TAP2 Expressed by Recombinant Vaccinia Viruses (∗). Journal Of Biological Chemistry 1995, 270: 21312-21318. PMID: 7673167, DOI: 10.1074/jbc.270.36.21312.Peer-Reviewed Original ResearchMeSH KeywordsATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCell LineDetergentsFluorescent Antibody TechniqueGlycosylationHumansMajor Histocompatibility ComplexMicroscopy, ConfocalNucleotidesProtein BindingRecombination, GeneticVaccinia virus
1994
In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides
Avva R, Cresswell P. In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides. Immunity 1994, 1: 763-774. PMID: 7895165, DOI: 10.1016/s1074-7613(94)80018-9.Peer-Reviewed Original ResearchConceptsHLA-DM expressionDR alpha beta dimersHLA-DR moleculesCLIP dissociationClass II moleculesHLA-DR complexInvariant chain peptideII-peptide complexesPrimary aliphatic aminesResidual fragmentsChain-derived peptideClass IIHLA-DMAliphatic aminesCarboxylic acidsSuch complexesUnbranched hydrocarbonsAlpha beta dimersChain peptideInvariant chain-derived peptidesComplexesVivoCLIP complexBeta dimersDissociationAssembly and intracellular transport of HLA-DM and correction of the class II antigen-processing defect in T2 cells
Denzin L, Robbins N, Carboy-Newcomb C, Cresswell P. Assembly and intracellular transport of HLA-DM and correction of the class II antigen-processing defect in T2 cells. Immunity 1994, 1: 595-606. PMID: 7600288, DOI: 10.1016/1074-7613(94)90049-3.Peer-Reviewed Original ResearchAntigen PresentationAntigens, Differentiation, B-LymphocyteBase SequenceBiological TransportCell LineCell MembraneFlow CytometryHistocompatibility Antigens Class IIHLA-D AntigensHLA-DR3 AntigenHumansHybrid CellsKineticsMolecular Sequence DataMutationNeoplasm ProteinsPrecipitin TestsSodium Dodecyl SulfateTime FactorsTransfectionHuman transporters associated with antigen processing possess a promiscuous peptide-binding site
Androlewicz M, Cresswell P. Human transporters associated with antigen processing possess a promiscuous peptide-binding site. Immunity 1994, 1: 7-14. PMID: 7889401, DOI: 10.1016/1074-7613(94)90004-3.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceAntigen PresentationATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBinding SitesBinding, CompetitiveBiological Transport, ActiveCarrier ProteinsCell LineHistocompatibility Antigens Class IHumansMolecular Sequence DataOligopeptidesMHC 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
HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides
Riberdy J, Newcomb J, Surman M, Barbosat J, Cresswell P. HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides. Nature 1992, 360: 474-477. PMID: 1448172, DOI: 10.1038/360474a0.Peer-Reviewed Original ResearchConceptsClass II moleculesInvariant chainMajor histocompatibility complex (MHC) class II moleculesCell linesHLA-DR moleculesClass II binding siteInvariant chain peptideHLA-DR3 moleculesMore MHCClass IIAntigen processingT2 transfectantsAntigenic peptidesHuman cell linesChain peptideVivo conditionsPeptidesLarge proportionProteolytic cleavageMutant cell linesCertain human cell linesEarly stagesTransfectantsProteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules
Arnold D, Driscoll J, Androlewicz M, Hughes E, Cresswell P, Spies T. Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules. Nature 1992, 360: 171-174. PMID: 1436094, DOI: 10.1038/360171a0.Peer-Reviewed Original ResearchAntigen-Antibody ReactionsAntigens, ViralATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCarrier ProteinsCell LineChromatography, High Pressure LiquidCysteine EndopeptidasesElectrophoresis, Gel, Two-DimensionalHistocompatibility Antigens Class IHistocompatibility Antigens Class IIHLA-A AntigensHLA-B AntigensHumansMembrane ProteinsMultienzyme ComplexesProteasome Endopeptidase ComplexProteinsT-LymphocytesTransfectionViral Matrix Proteins