2024
Cutting Edge: Phagosome-associated Autophagosomes Containing Antigens and Proteasomes Drive TAP-Independent Cross-Presentation.
Sengupta D, Galicia-Pereyra R, Han P, Graham M, Liu X, Arshad N, Cresswell P. Cutting Edge: Phagosome-associated Autophagosomes Containing Antigens and Proteasomes Drive TAP-Independent Cross-Presentation. The Journal Of Immunology 2024, 212: 1063-1068. PMID: 38353614, PMCID: PMC10948299, DOI: 10.4049/jimmunol.2200446.Peer-Reviewed Original ResearchCross-presentationTransporter associated with Ag processingExogenous AgCD8-positive T lymphocytesAntigenic peptidesMHC-I moleculesDendritic cellsProteasomal deliveryT lymphocytesCytosolic proteasomeActive proteasomesEndocytic compartmentsTAP-independentLumen of phagosomesSubcellular compartmentsEndoplasmic reticulumEndolysosomal vesiclesMHC-IAg processingBind to MHC-IProteasome
2022
SARS-CoV-2 accessory proteins ORF7a and ORF3a use distinct mechanisms to down-regulate MHC-I surface expression
Arshad N, Laurent-Rolle M, Ahmed W, Hsu J, Mitchell S, Pawlak J, Sengupta D, Biswas K, Cresswell P. SARS-CoV-2 accessory proteins ORF7a and ORF3a use distinct mechanisms to down-regulate MHC-I surface expression. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 120: e2208525120. PMID: 36574644, PMCID: PMC9910621, DOI: 10.1073/pnas.2208525120.Peer-Reviewed Original ResearchConceptsMHC-I expressionSARS-CoV-2Major histocompatibility complex (MHC) class I moleculesT cell recognitionVirus-infected cellsClass I moleculesAntigen presentationOngoing COVID-19 pandemicHeavy chainImmune evasionViral peptidesSecretory pathwayDistinct mechanismsMHCI moleculesPeptide-MHCInfected cellsCausative agentCell recognitionCD8COVID-19 pandemicViral proteinsEndoplasmic reticulumHuman MHCORF7a
2017
Antigen Processing and Presentation Mechanisms in Myeloid Cells
Roche P, Cresswell P. Antigen Processing and Presentation Mechanisms in Myeloid Cells. 2017, 209-223. DOI: 10.1128/9781555819194.ch11.Peer-Reviewed Original ResearchDendritic cellsAntigen processingMHC-IIMyeloid cellsMHC-II-associated peptidesEffective adaptive immune responseMajor histocompatibility complex class IHistocompatibility complex class IAdaptive immune responsesAntigen-derived peptidesClass II moleculesComplex class IImmune responseMHC moleculesMHC glycoproteinsMHCClass IEndocytosis of antigensMature effectorsEndolysosomal systemPeptide generationTransmembrane glycoproteinEndoplasmic reticulumCellsPresentation
2001
Quality control of transmembrane domain assembly in the tetraspanin CD82
Cannon K, Cresswell P. Quality control of transmembrane domain assembly in the tetraspanin CD82. The EMBO Journal 2001, 20: 2443-2453. PMID: 11350933, PMCID: PMC125455, DOI: 10.1093/emboj/20.10.2443.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumTransmembrane segmentsDomain assemblyER quality controlFirst transmembrane segmentMore transmembrane segmentsER membraneER lumenChaperone calnexinSeparate polypeptidesTetraspanin CD82TM-1Extracellular domainCalnexinNative structureCell surfaceTM-2Lipid bilayersCD82AssemblyQuality controlPrimary mechanismProlonged interactionPolypeptideCalreticulin
1999
The nature of the MHC class I peptide loading complex
Cresswell P, Bangia N, Dick T, Diedrich G. The nature of the MHC class I peptide loading complex. Immunological Reviews 1999, 172: 21-28. PMID: 10631934, DOI: 10.1111/j.1600-065x.1999.tb01353.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigen PresentationATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersDimerizationEndoplasmic ReticulumHistocompatibility Antigens Class IHumansModels, MolecularPeptidesProtein BindingProtein Structure, Quaternary
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 virusGenomic 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 moleculePhylogenyIntronsChromosomesESTs
1997
Protein degradation: The ins and outs of the matter
Cresswell P, Hughes E. Protein degradation: The ins and outs of the matter. Current Biology 1997, 7: r552-r555. PMID: 9285707, DOI: 10.1016/s0960-9822(06)00279-x.Peer-Reviewed Original ResearchMisfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome
Hughes E, Hammond C, Cresswell P. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1896-1901. PMID: 9050876, PMCID: PMC20014, DOI: 10.1073/pnas.94.5.1896.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteineBeta 2-MicroglobulinBlotting, WesternCysteine EndopeptidasesCysteine Proteinase InhibitorsCytoplasmEndoplasmic ReticulumEnzyme InhibitorsGlycosylationHistocompatibility Antigens Class IHumansKineticsLeupeptinsMultienzyme ComplexesProteasome Endopeptidase ComplexProtein FoldingSolubilityTransfectionTumor Cells, CulturedConceptsClass I heavy chainsMHC class I heavy chainMajor histocompatibility complex class I heavy chainsBeta2-microglobulinHeavy chainMHC class ICell linesCell line DaudiTAP-deficient cell linesSpecific irreversible inhibitorClass IHerpes simplex virus proteinDaudiVirus proteinsEndoplasmic reticulumIrreversible inhibitorSimilar accumulationLactacystinPeriod of hours
1994
Assembly, Transport, and Function of MHC Class II Molecules
Cresswell P. Assembly, Transport, and Function of MHC Class II Molecules. Annual Review Of Immunology 1994, 12: 259-291. PMID: 8011283, DOI: 10.1146/annurev.iy.12.040194.001355.Peer-Reviewed Original ResearchConceptsII-invariant chain complexesEndosomal systemMembrane protein transportTrans-Golgi networkCell surfaceChain complexesAdditional gene productsAlpha beta dimersLate endosome/Beta dimersProtein transportCytoplasmic tailGene productsConstitutive pathwayEndosome/Golgi apparatusEndoplasmic reticulumInvariant chainMHC class II moleculesPrimary functionPrecise mechanismClass II moleculesComplexesPeptidesBind peptides