2022
Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation
Jiang J, Taylor DK, Kim EJ, Boyd LF, Ahmad J, Mage MG, Truong HV, Woodward CH, Sgourakis NG, Cresswell P, Margulies DH, Natarajan K. Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation. Nature Communications 2022, 13: 5470. PMID: 36115831, PMCID: PMC9482634, DOI: 10.1038/s41467-022-33153-8.Peer-Reviewed Original Research
2001
Glycosylation and the Immune System
Rudd P, Elliott T, Cresswell P, Wilson I, Dwek R. Glycosylation and the Immune System. Science 2001, 291: 2370-2376. PMID: 11269318, DOI: 10.1126/science.291.5512.2370.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigen PresentationAntigen-Antibody ReactionsAntigen-Presenting CellsAntigens, CD1Carrier ProteinsCollectinsComplement System ProteinsEndoplasmic ReticulumEpitopesGlycoproteinsGlycosylationHistocompatibility AntigensHumansImmune SystemImmunoglobulinsPolysaccharidesProtein FoldingT-LymphocytesViral Envelope ProteinsConceptsImmune systemMajor histocompatibility complex antigensAntigen-presenting cellsAdaptive immune responsesCellular immune systemHistocompatibility complex antigensHumoral immune systemT cell receptor complexRheumatoid arthritisMannose-binding lectinAutoimmune diseasesCell receptor complexT cellsImmune responseComplex antigensPeptide antigensComplement componentsImmunoglobulin GAntigenKey moleculesReceptor complexSpecific glycoformsGlycoproteinGlycopeptide antigensArthritisA Role for Calnexin in the Assembly of the MHC Class I Loading Complex in the Endoplasmic Reticulum
Diedrich G, Bangia N, Pan M, Cresswell P. A Role for Calnexin in the Assembly of the MHC Class I Loading Complex in the Endoplasmic Reticulum. The Journal Of Immunology 2001, 166: 1703-1709. PMID: 11160214, DOI: 10.4049/jimmunol.166.3.1703.Peer-Reviewed Original ResearchAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersCalcium-Binding ProteinsCalnexinCalreticulinCell Line, TransformedDimerizationEndoplasmic ReticulumHeat-Shock ProteinsHeLa CellsHistocompatibility Antigens Class IHLA AntigensHumansImmunoglobulinsIsomerasesKineticsMajor Histocompatibility ComplexMembrane Transport ProteinsProtein BindingProtein Disulfide-IsomerasesRibonucleoproteinsTumor Cells, Cultured
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 virusThe thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
Hughes E, Cresswell P. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Current Biology 1998, 8: 709-713. PMID: 9637923, DOI: 10.1016/s0960-9822(98)70278-7.Peer-Reviewed Original ResearchAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersCalcium-Binding ProteinsCalreticulinEndoplasmic ReticulumHeat-Shock ProteinsHeLa CellsHistocompatibility Antigens Class IHumansImmunoglobulinsIsomerasesMembrane Transport ProteinsPeptidesProtein Disulfide Reductase (Glutathione)Protein Disulfide-IsomerasesRibonucleoproteinsHLA-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 PropertiesTransfectionGenomic 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 moleculePhylogenyIntronsChromosomesESTsSoluble Tapasin Restores MHC Class I Expression and Function in the Tapasin-Negative Cell Line .220
Lehner P, Surman M, Cresswell P. Soluble Tapasin Restores MHC Class I Expression and Function in the Tapasin-Negative Cell Line .220. Immunity 1998, 8: 221-231. PMID: 9492003, DOI: 10.1016/s1074-7613(00)80474-4.Peer-Reviewed Original ResearchAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersBiological TransportEndoplasmic ReticulumHLA-B8 AntigenHumansImmunoglobulinsMembrane Transport ProteinsMutationPeptidesProtein BindingSolubilityT-Lymphocytes, Cytotoxic
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 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
1987
Localization of an epitope of beta-2 microglobulin that is shared with other members of the immunoglobulin superfamily
Parham P, Lutz P, Cresswell P. Localization of an epitope of beta-2 microglobulin that is shared with other members of the immunoglobulin superfamily. Immunogenetics 1987, 26: 323-326. PMID: 2443449, DOI: 10.1007/bf00346533.Peer-Reviewed Original Research
1974
The Immunoglobulin‐Like Structure of Human Histocompatibility Antigens
Strominger J, Cresswell P, Grey H, Humphreys R, Mann D, Mccune J, Parham P, Robb R, Sanderson A, Springer T, Terhorst C, Turner M. The Immunoglobulin‐Like Structure of Human Histocompatibility Antigens. Immunological Reviews 1974, 21: 126-143. PMID: 4139785, DOI: 10.1111/j.1600-065x.1974.tb01549.x.Peer-Reviewed Original ResearchAntigen-Antibody ComplexBeta-GlobulinsCarbon RadioisotopesCell LineCell MembraneCells, CulturedChromatographyChromatography, GelDetergentsElectrophoresisHistocompatibility AntigensImmune SeraImmunoglobulinsIodine RadioisotopesIsoantibodiesIsoelectric FocusingLymphocyte ActivationLymphocytesMolecular WeightNeuraminidasePapainTritium
1971
THE CYTOTOXIC EFFECT ON HUMAN LYMPHOCYTES OF RABBIT ANTISERA TO HUMAN FC (IGG)
WELSH K, CRESSWELL P, GOUJET C, SANDERSON A. THE CYTOTOXIC EFFECT ON HUMAN LYMPHOCYTES OF RABBIT ANTISERA TO HUMAN FC (IGG). Transplantation 1971, 12: 468-471. PMID: 5165966, DOI: 10.1097/00007890-197112000-00009.Peer-Reviewed Original Research