2023
A membrane-associated MHC-I inhibitory axis for cancer immune evasion
Chen X, Lu Q, Zhou H, Liu J, Nadorp B, Lasry A, Sun Z, Lai B, Rona G, Zhang J, Cammer M, Wang K, Al-Santli W, Ciantra Z, Guo Q, You J, Sengupta D, Boukhris A, Zhang H, Liu C, Cresswell P, Dahia P, Pagano M, Aifantis I, Wang J. A membrane-associated MHC-I inhibitory axis for cancer immune evasion. Cell 2023, 186: 3903-3920.e21. PMID: 37557169, PMCID: PMC10961051, DOI: 10.1016/j.cell.2023.07.016.Peer-Reviewed Original ResearchMeSH KeywordsAntigen PresentationCD8-Positive T-LymphocytesHistocompatibility Antigens Class IHLA AntigensHumansNeoplasmsTumor EscapeUbiquitin-Protein LigasesConceptsAcute myeloid leukemiaSolid cancersImmune evasionCancer immune evasionImmune checkpoint blockadeMultiple solid cancersMajor Histocompatibility Complex Class I Antigen PresentationPotential therapeutic targetCell-dependent mannerCell immunityCancer survivalMyeloid leukemiaAntigen presentationTherapeutic targetTransmembrane protein 127Tumor growthGene signatureCancer treatmentCancerPeptide-MHCMHCLeukemiaSushi domainTrimolecular complexE3 ubiquitin ligase WWP2
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 ResearchMeSH KeywordsAntigen PresentationCOVID-19Histocompatibility Antigens Class IHLA AntigensHumansPeptidesSARS-CoV-2Viral Regulatory and Accessory ProteinsConceptsMHC-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 MHCORF7aStructural 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
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-LymphocytesGlycosylation 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 antigensArthritisAntigen processing and recognition
Cresswell P, Lanzavecchia A. Antigen processing and recognition. Current Opinion In Immunology 2001, 13: 11-12. PMID: 11154910, DOI: 10.1016/s0952-7915(00)00174-6.Peer-Reviewed Original Research
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, QuaternaryCytomegalovirus US2 destroys two components of the MHC class II pathway, preventing recognition by CD4+ T cells
Tomazin R, Boname J, Hegde N, Lewinsohn D, Altschuler Y, Jones T, Cresswell P, Nelson J, Riddell S, Johnson D. Cytomegalovirus US2 destroys two components of the MHC class II pathway, preventing recognition by CD4+ T cells. Nature Medicine 1999, 5: 1039-1043. PMID: 10470081, DOI: 10.1038/12478.Peer-Reviewed Original ResearchConceptsHuman cytomegalovirusT cellsT lymphocytesClass II proteinsMHC class II antigen presentation pathwayMHC class II pathwayClass II antigen presentation pathwayHCMV-infected macrophagesAntigen presentation pathwayClass II pathwayLifelong latent infectionLife-threatening diseaseMonocytes/macrophagesMHC class IImportant host cellsMHC class II proteinsImmune evasion proteinsVirus reactivationHLA-DRLatent reservoirPresent antigensGlial cellsUbiquitous herpesvirusLatent infectionPresentation pathwayThiol 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 ResearchThe 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-IsomerasesRibonucleoproteinsHuman epidermal Langerhans cells lack functional mannose receptors and a fully developed endosomal/lysosomal compartment for loading of HLA class II molecules
Mommaas A, Mulder A, Jordens R, Out C, Tan M, Cresswell P, Kluin P, Koning F. Human epidermal Langerhans cells lack functional mannose receptors and a fully developed endosomal/lysosomal compartment for loading of HLA class II molecules. European Journal Of Immunology 1999, 29: 571-580. PMID: 10064073, DOI: 10.1002/(sici)1521-4141(199902)29:02<571::aid-immu571>3.0.co;2-e.Peer-Reviewed Original ResearchConceptsHuman epidermal Langerhans cellsEpidermal Langerhans cellsLangerhans cellsT cellsAntigen-specific T cellsMannose receptorPeripheral blood mononuclear cellsHLA class II moleculesProtein antigensBlood-derived DCsBlood mononuclear cellsAntigen-presenting cellsNaive T cellsDendritic cell lineageClass II moleculesClass II compartmentsFunctional mannose receptorsLymph nodesAntigen uptakeMononuclear cellsMHC classEndocytic capacitySkin damageReceptor-mediated endocytosis pathwayAntigenAntigen recognition Editorial overview
Cresswell P, Howard J. Antigen recognition Editorial overview. Current Opinion In Immunology 1999, 11: 61-63. PMID: 10084794, DOI: 10.1016/s0952-7915(99)80011-9.Peer-Reviewed Original Research
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 moleculesHeterodimersHLA-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 ResearchMECHANISMS OF MHC CLASS I–RESTRICTED ANTIGEN PROCESSING
Pamer E, Cresswell P. MECHANISMS OF MHC CLASS I–RESTRICTED ANTIGEN PROCESSING. Annual Review Of Immunology 1998, 16: 323-358. PMID: 9597133, DOI: 10.1146/annurev.immunol.16.1.323.Peer-Reviewed Original ResearchSoluble 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, CytotoxicQuantitative 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
1997
Negative Regulation by HLA-DO of MHC Class II-Restricted Antigen Processing
Denzin L, Sant'Angelo D, Hammond C, Surman M, Cresswell P. Negative Regulation by HLA-DO of MHC Class II-Restricted Antigen Processing. Science 1997, 278: 106-109. PMID: 9311912, DOI: 10.1126/science.278.5335.106.Peer-Reviewed Original ResearchConceptsHLA-DOII-like moleculeAntigen processingClass IIHLA-DMMajor histocompatibility complex classMHC class IIHistocompatibility complex classClass II moleculesII-CLIP complexesHLA-DM functionT cell linesB cellsChain-derived peptideAntigenic peptidesImportant modulatorCell linesDM functionInvariant chain-derived peptidesComplex classNegative regulationPeptidesA 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