Najla Arshad, PhD
About
Research
Publications
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
2021
Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease
Arshad N, Cresswell P. Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease. Progress In Molecular And Subcellular Biology 2021, 59: 163-180. PMID: 34050866, DOI: 10.1007/978-3-030-67696-4_8.ChaptersConceptsEndoplasmic reticulumProtein quality control machineryER-resident protein calreticulinQuality control machineryKey cellular functionsAmino acid sequenceEndoplasmic reticulum functionLectin chaperonesCellular functionsControl machineryProtein interactionsTerminal domainER healthER functionAcid sequenceMutant calreticulinCell homeostasisProtein calreticulinProtein synthesisCalreticulinVital playersDramatic alterationsLipid metabolismBlood tumorsMutations
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
2019
Extracorporeal photochemotherapy induces bona fide immunogenic cell death
Tatsuno K, Yamazaki T, Hanlon D, Han P, Robinson E, Sobolev O, Yurter A, Rivera-Molina F, Arshad N, Edelson RL, Galluzzi L. Extracorporeal photochemotherapy induces bona fide immunogenic cell death. Cell Death & Disease 2019, 10: 578. PMID: 31371700, PMCID: PMC6675789, DOI: 10.1038/s41419-019-1819-3.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsAntigens, NeoplasmApoptosisCD8-Positive T-LymphocytesCell DifferentiationCell Line, TumorCell SurvivalDendritic CellsHMGB1 ProteinHumansImmunogenic Cell DeathLeukocytesLymphoma, T-Cell, CutaneousMethoxsalenMiceMonocytesPhotopheresisPhotosensitizing AgentsReceptor, Interferon alpha-betaUltraviolet RaysConceptsHigh mobility group box 1Tumor-associated antigensCutaneous T-cell lymphomaWhite blood cellsDendritic cellsImmunostimulatory signalsI interferonBona fide immunogenic cell deathMobility group box 1Such dendritic cellsSyngeneic immunocompetent miceCancer cellsT-cell lymphomaType I IFN receptorGroup box 1Immunogenic cell deathI IFN receptorATP-degrading enzymeSecretion of ATPMelanoma cell viabilityCognate immunityUVA irradiationAnticancer immunityImmunocompetent miceCalreticulin exposure
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 ResearchConceptsMyeloproliferative 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
2017
The Role of ER‐resident Lectin Chaperone UGT1 in MHC Class I Peptide Loading
Arshad N, Cresswell P. The Role of ER‐resident Lectin Chaperone UGT1 in MHC Class I Peptide Loading. The FASEB Journal 2017, 31 DOI: 10.1096/fasebj.31.1_supplement.604.13.Peer-Reviewed Original Research
2013
Cyclic nucleotide signaling in intestinal epithelia: getting to the gut of the matter
Arshad N, Visweswariah SS. Cyclic nucleotide signaling in intestinal epithelia: getting to the gut of the matter. WIREs Mechanisms Of Disease 2013, 5: 409-424. PMID: 23610087, DOI: 10.1002/wsbm.1223.Peer-Reviewed Original ResearchConceptsIntestinal epithelial cell homeostasisEpithelial cell homeostasisCyclic AMPCyclic nucleotidesWeb of interactionsNucleotidyl cyclasesSymbiotic microbiotaTranscription factorsProtein kinaseIntestinal epitheliumDownstream effectorsCell homeostasisDiverse processesIntestinal epithelial cellsSecond messengerCyclic GMPIon channelsNutrient absorptionIntrinsic cuesCell proliferationNeoplastic growthEpithelial cellsPathwayNucleotidesKey processes
2012
Site-specific N-Linked Glycosylation of Receptor Guanylyl Cyclase C Regulates Ligand Binding, Ligand-mediated Activation and Interaction with Vesicular Integral Membrane Protein 36, VIP36*
Arshad N, Ballal S, Visweswariah SS. Site-specific N-Linked Glycosylation of Receptor Guanylyl Cyclase C Regulates Ligand Binding, Ligand-mediated Activation and Interaction with Vesicular Integral Membrane Protein 36, VIP36*. Journal Of Biological Chemistry 2012, 288: 3907-3917. PMID: 23269669, PMCID: PMC3567644, DOI: 10.1074/jbc.m112.413906.Peer-Reviewed Original ResearchMeSH KeywordsCell LineCell MembraneEndoplasmic ReticulumGastrointestinal HormonesGlycosylationHumansLigandsMannose-Binding LectinsMembrane Transport ProteinsNatriuretic PeptidesProtein BindingProtein FoldingProtein Structure, TertiaryReceptors, EnterotoxinReceptors, Guanylate Cyclase-CoupledReceptors, PeptideConceptsLigand bindingVesicular integral membrane proteinGuanylyl cyclase CIntegral membrane proteinsGlycosylation of proteinsHeat‐stable enterotoxin peptideLigand-mediated activationSite of glycosylationTissue-dependent mannerReceptor guanylyl cyclaseReceptor guanylyl cyclase CGlycan-mediated interactionsDifferent cell typesMembrane proteinsSystematic mutagenesisGlycosylation sitesCyclase CCGMP-dependent mannerExtracellular domainProtein 36Endoplasmic reticulumSurface localizationVIP36Cell typesST peptidesThe multiple and enigmatic roles of guanylyl cyclase C in intestinal homeostasis
Arshad N, Visweswariah SS. The multiple and enigmatic roles of guanylyl cyclase C in intestinal homeostasis. FEBS Letters 2012, 586: 2835-2840. PMID: 22819815, DOI: 10.1016/j.febslet.2012.07.028.Peer-Reviewed Original ResearchConceptsGuanylyl cyclase CCyclase CGut immune systemIntestinal epithelial cellsColon cell proliferationTravelers' diarrheaIntestinal homeostasisHeat-stable enterotoxinImmune systemActivation of GCIon secretionEpithelial cellsCell proliferationCausative agentDiarrheaIntracellular levelsFirst descriptionReceptorsRecent findingsFuture studiesHuman diseasesEnigmatic roleNew findingsDiseaseFindings