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
Proteasomal degradation within endocytic organelles can mediate antigen cross- presentation
Sengupta D, Graham M, Liu X, Cresswell P. Proteasomal degradation within endocytic organelles can mediate antigen cross- presentation. Molecular Immunology 2022, 150: 23. DOI: 10.1016/j.molimm.2022.05.080.Peer-Reviewed Original ResearchDendritic cellsMHC-I moleculesMouse bone marrow-derived dendritic cellsBone marrow-derived dendritic cellsMarrow-derived dendritic cellsAntigen processingConventional antigen processingMouse dendritic cellsMHC-I-peptide complexesSurface MHCMHCSurface expressionProteasome inhibitionPeptide loadingHuman B2Cell phagosomesCell typesActive proteasomesSpecific peptidesCellsPeptidesEndocytic compartmentsProteasomal degradationEndocytic pathway
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
Cathepsin S Regulates the Expression of Cathepsin L and the Turnover of γ-Interferon-inducible Lysosomal Thiol Reductase in B Lymphocytes*
Honey K, Duff M, Beers C, Brissette W, Elliott E, Peters C, Maric M, Cresswell P, Rudensky A. Cathepsin S Regulates the Expression of Cathepsin L and the Turnover of γ-Interferon-inducible Lysosomal Thiol Reductase in B Lymphocytes*. Journal Of Biological Chemistry 2001, 276: 22573-22578. PMID: 11306582, DOI: 10.1074/jbc.m101851200.Peer-Reviewed Original ResearchConceptsB cellsCathepsin SMajor histocompatibility complex (MHC) class II moleculesClass II presentation pathwayT cell responsesPeripheral lymphoid organsCathepsin L proteinClass II moleculesInvariant chain cleavageAntigenic peptide fragmentsDendritic cellsLymphoid organsLysosomal thiol reductaseAntigen presentationPresentation pathwayB lymphocytesCell responsesMature giltsΓ-interferon-inducible lysosomal thiol reductaseInvariant chainThiol reductaseInducible lysosomal thiol reductaseNovel mechanismCathepsin LCells