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 ResearchConceptsAcute 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 WWP2CMPK2 restricts Zika virus replication by inhibiting viral translation
Pawlak J, Hsu J, Xia H, Han P, Suh H, Grove T, Morrison J, Shi P, Cresswell P, Laurent-Rolle M. CMPK2 restricts Zika virus replication by inhibiting viral translation. PLOS Pathogens 2023, 19: e1011286. PMID: 37075076, PMCID: PMC10150978, DOI: 10.1371/journal.ppat.1011286.Peer-Reviewed Original ResearchConceptsCytidine/uridine monophosphate kinase 2I interferon-stimulated genesZika virus replicationYellow fever virusAntiviral activityAntiviral effectVirus replicationKunjin virusType I interferon-stimulated genesFirst lineOverall antiviral responseHost's first lineEffective therapeutic interventionsViral translationBroad antiviral activityInterferon-stimulated genesGlobal health threatAntiviral treatmentFlaviviral infectionsPathogenic flavivirusesAntiviral functionDrug AdministrationTherapeutic interventionsAntiviral responseDengue virus
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 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
Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus
Chin K, Cresswell P. Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 15125-15130. PMID: 11752458, PMCID: PMC64994, DOI: 10.1073/pnas.011593298.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCells, CulturedCytomegalovirusDNA, ComplementaryHumansInterferon-alphaInterferon-betaMolecular Sequence DataOxidoreductases Acting on CH-CH Group DonorsProtein BiosynthesisProteinsSequence Homology, Amino AcidViral Envelope ProteinsVirus ReplicationMaintenance of TCR clonality in T cells expressing genes for two TCR heterodimers
Sant'Angelo D, Cresswell P, Janeway C, Denzin L. Maintenance of TCR clonality in T cells expressing genes for two TCR heterodimers. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 6824-6829. PMID: 11381132, PMCID: PMC34437, DOI: 10.1073/pnas.121179998.Peer-Reviewed Original ResearchConceptsAllelic exclusionTCR heterodimerTCR proteinsCell surface expressionTCR lociT cellsCell surfaceFurther recombinationProteinAlpha chainBeta chainHeterodimersSurface expressionTransgenic miceTCR transgenic miceCellsAdditional mechanismExpressionTCR clonalityAssembly processGenesSecond TCRLociRNATCRDistinct 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 ProteinsTransfectionMultiple species express thiol oxidoreductases related to GILT
Phan U, Maric M, Dick T, Cresswell P. Multiple species express thiol oxidoreductases related to GILT. Immunogenetics 2001, 53: 342-346. PMID: 11491538, DOI: 10.1007/s002510100323.Peer-Reviewed Original ResearchGlycosylation 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, CulturedAntigen 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
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 ResearchInteraction of Human Immunodeficiency Virus Type 2 Vpx and Invariant Chain
Pancio H, Vander Heyden N, Kosuri K, Cresswell P, Ratner L. Interaction of Human Immunodeficiency Virus Type 2 Vpx and Invariant Chain. Journal Of Virology 2000, 74: 6168-6172. PMID: 10846101, PMCID: PMC112116, DOI: 10.1128/jvi.74.13.6168-6172.2000.Peer-Reviewed Original ResearchConceptsMajor histocompatibility complex class II antigen presentationHuman immunodeficiency virus type 2Class II antigen presentationHIV-2 VpxSimian immunodeficiency virusInvariant chainVirus type 2Immunodeficiency virusAntigen presentationVirion-associated proteinType 2VpxInfected cellsCellsFusion proteinCellular proteinsProteinS-transferase fusion proteinIntracellular Surveillance: Controlling the Assembly of MHC Class I‐Peptide Complexes
Cresswell P. Intracellular Surveillance: Controlling the Assembly of MHC Class I‐Peptide Complexes. Traffic 2000, 1: 301-305. PMID: 11208114, DOI: 10.1034/j.1600-0854.2000.010402.x.Peer-Reviewed Original ResearchEnzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GILT)
Arunachalam B, Phan U, Geuze H, Cresswell P. Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GILT). Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 745-750. PMID: 10639150, PMCID: PMC15401, DOI: 10.1073/pnas.97.2.745.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesCOS CellsDisulfidesDNA, ComplementaryEndosomesEnzyme InductionHumansHydrogen-Ion ConcentrationInterferon-gammaLysosomesMannosephosphatesMicroscopy, ImmunoelectronMolecular Sequence DataMutagenesisOxidation-ReductionProtein Disulfide Reductase (Glutathione)Protein Processing, Post-TranslationalSequence Analysis, DNATumor Cells, CulturedConceptsGamma interferon inducible lysosomal thiol reductaseLysosomal thiol reductaseThiol reductaseDisulfide bondsC-terminal prosequenceEndocytic pathwayThioredoxin familyCysteine residuesDisulfide bond reductionEfficient proteolysisCell typesAmino acidsLysosomal systemEnzymeLysosomesSoluble glycoproteinReductaseActive siteBond reductionAntigen processingImportant roleEnzymatic reductionMutagenesisThioredoxinProsequence
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 pathwayThe 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