2024
mosGILT controls innate immunity and germ cell development in Anopheles gambiae
Arora G, Tang X, Cui Y, Yang J, Chuang Y, Joshi J, Sajid A, Dong Y, Cresswell P, Dimopoulos G, Fikrig E. mosGILT controls innate immunity and germ cell development in Anopheles gambiae. BMC Genomics 2024, 25: 42. PMID: 38191283, PMCID: PMC10775533, DOI: 10.1186/s12864-023-09887-0.Peer-Reviewed Original ResearchConceptsGerm cell developmentAnopheles gambiaeCell developmentOvarian developmentReductase-like proteinWild-type mosquitoesPlasmodium life cycleBiological controlGrowth genesEssential regulatorRNA sequencingA. gambiaeGenesGambiaeAltered expressionImpaired ovarian developmentMosquito vectorsLife cycleMosquitoesImmune activationPlasmodium infectionTranscriptomeOogenesisRegulatorProtein
2023
CMPK2 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
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 ReplicationDefective 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-LymphocytesDistinct 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 ProteinsTransfectionQuality control of transmembrane domain assembly in the tetraspanin CD82
Cannon K, Cresswell P. Quality control of transmembrane domain assembly in the tetraspanin CD82. The EMBO Journal 2001, 20: 2443-2453. PMID: 11350933, PMCID: PMC125455, DOI: 10.1093/emboj/20.10.2443.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumTransmembrane segmentsDomain assemblyER quality controlFirst transmembrane segmentMore transmembrane segmentsER membraneER lumenChaperone calnexinSeparate polypeptidesTetraspanin CD82TM-1Extracellular domainCalnexinNative structureCell surfaceTM-2Lipid bilayersCD82AssemblyQuality controlPrimary mechanismProlonged interactionPolypeptideCalreticulinMultiple 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 ResearchCathepsin 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 LCellsGlycosylation 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
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 ResearchIntracellular 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, QuaternaryThiol 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 Research
1998
The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules.
Hammond C, Denzin L, Pan M, Griffith J, Geuze H, Cresswell P. The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules. The Journal Of Immunology 1998, 161: 3282-91. PMID: 9759843, DOI: 10.4049/jimmunol.161.7.3282.Peer-Reviewed Original ResearchAssembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors.
Deng Y, Gibbs J, Bačík I, Porgador A, Copeman J, Lehner P, Ortmann B, Cresswell P, Bennink J, Yewdell J. Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors. The Journal Of Immunology 1998, 161: 1677-85. PMID: 9712031, DOI: 10.4049/jimmunol.161.4.1677.Peer-Reviewed Original ResearchMeSH KeywordsAedesAnimalsAntibodies, MonoclonalAntiportersCell LineEndoplasmic ReticulumH-2 AntigensHeLa CellsHumansImmunoglobulinsLymphocyte ActivationMacromolecular SubstancesMembrane Transport ProteinsMiceOligopeptidesOvalbuminPeptide FragmentsProtease InhibitorsRecombinant ProteinsT-LymphocytesVaccinia virusConceptsInsect cellsEndoplasmic reticulumVertebrate cellsHuman cellsHuman tapasinVaccinia virus-mediated expressionCell surface expressionProtease inhibitorsInefficient assemblyKbMHC class IMouse betaInsectsEfficient assemblyImmediate precursorSurface expressionAntigenic peptidesHeavy chainClass IRecombinant vaccinia virusVirus-mediated expressionAssemblyExpressionCellsVaccinia virusIntracellular formation and cell surface expression of a complex of an intact lysosomal protein and MHC class II molecules.
Arunachalam B, Pan M, Cresswell P. Intracellular formation and cell surface expression of a complex of an intact lysosomal protein and MHC class II molecules. The Journal Of Immunology 1998, 160: 5797-806. PMID: 9637490, DOI: 10.4049/jimmunol.160.12.5797.Peer-Reviewed Original ResearchAllelesAnimalsCell Transformation, ViralElectrophoresis, Polyacrylamide GelFlow CytometryFluorescent Antibody Technique, IndirectHerpesvirus 4, HumanHistocompatibility Antigens Class IIHLA-D AntigensHLA-DR AntigensLysosomesMiceOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsProteinsRabbitsSodium Dodecyl SulfateSurface PropertiesHLA-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 Research