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 MHCORF7a
2020
Platelet P-selectin initiates cross-presentation and dendritic cell differentiation in blood monocytes
Han P, Hanlon D, Arshad N, Lee JS, Tatsuno K, Yurter A, Robinson E, Filler R, Sobolev O, Cote C, Rivera-Molina F, Toomre D, Fahmy T, Edelson R. Platelet P-selectin initiates cross-presentation and dendritic cell differentiation in blood monocytes. Science Advances 2020, 6: eaaz1580. PMID: 32195350, PMCID: PMC7065880, DOI: 10.1126/sciadv.aaz1580.Peer-Reviewed Original ResearchConceptsDendritic cellsDifferentiation of monocytesBlood monocytesTumor-specific T cell immunityCytokine-derived DCsT cell immunityAntigen-specific immunityPlatelet P-selectinDendritic cell differentiationPeripheral blood monocytesCell immunityP-selectin glycoprotein ligand-1P-selectinExogenous cytokinesNuclear factorMonocytesPhysiologic maturationPhysiological mannerCalcium fluxingNuclear localizationLigand 1Cell differentiationImmunityRapid maturationPlatelets
2018
Tumor-associated calreticulin variants functionally compromise the peptide loading complex and impair its recruitment of MHC-I
Arshad N, Cresswell P. Tumor-associated calreticulin variants functionally compromise the peptide loading complex and impair its recruitment of MHC-I. Journal Of Biological Chemistry 2018, 293: 9555-9569. PMID: 29769311, PMCID: PMC6016473, DOI: 10.1074/jbc.ra118.002836.Peer-Reviewed Original ResearchMeSH KeywordsAntigen PresentationCalreticulinHEK293 CellsHistocompatibility Antigens Class IHumansMutationNeoplasmsPeptide FragmentsSignal TransductionConceptsMyeloproliferative neoplasmsPeptide loading complexMHC-I levelsMajor histocompatibility complexEffective immunotherapyAntigen presentationImmune surveillanceImmune systemBlood tumorsSomatic frameshift mutationsTumor cellsMHCHistocompatibility complexSurface expressionGlycan-dependent mannerNeoplasmsTumorsNormal cellsReduced bindingHigh-affinity peptidesEndoplasmic reticulumBind peptidesCellsCalreticulinFrameshift mutation