2023
Plant MDL proteins synergize with the cytokine MIF at CXCR2 and CXCR4 receptors in human cells
Spiller L, Manjula R, Leissing F, Basquin J, Bourilhon P, Sinitski D, Brandhofer M, Levecque S, Gerra S, Sabelleck B, Zhang L, Feederle R, Flatley A, Hoffmann A, Panstruga R, Bernhagen J, Lolis E. Plant MDL proteins synergize with the cytokine MIF at CXCR2 and CXCR4 receptors in human cells. Science Signaling 2023, 16: eadg2621. PMID: 37988455, DOI: 10.1126/scisignal.adg2621.Peer-Reviewed Original ResearchConceptsMammalian macrophage migration inhibitory factorHetero-oligomeric complexesHigh structural similarityMultifunctional inflammatory cytokineHuman lung epithelial cellsYeast reporter systemReporter systemLung epithelial cellsPlant leavesFunctional similarityCellular responsesHuman cellsPharmacological inhibitorsDopachrome tautomeraseFunctional implicationsX-ray crystallographyMacrophage migration inhibitory factorStructural similarityEpithelial cellsMigration inhibitory factorCXCR4 receptorProteinTautomerase activityCellsMIF receptorMapping N- to C-terminal allosteric coupling through disruption of a putative CD74 activation site in D-dopachrome tautomerase
Chen E, Widjaja V, Kyro G, Allen B, Das P, Prahaladan V, Bhandari V, Lolis E, Batista V, Lisi G. Mapping N- to C-terminal allosteric coupling through disruption of a putative CD74 activation site in D-dopachrome tautomerase. Journal Of Biological Chemistry 2023, 299: 104729. PMID: 37080391, PMCID: PMC10208890, DOI: 10.1016/j.jbc.2023.104729.Peer-Reviewed Original Research
2022
A novel site on dual-specificity phosphatase MKP7/DUSP16 is required for catalysis and MAPK binding
Shillingford S, Zhang L, Surovtseva Y, Dorry S, Lolis E, Bennett AM. A novel site on dual-specificity phosphatase MKP7/DUSP16 is required for catalysis and MAPK binding. Journal Of Biological Chemistry 2022, 298: 102617. PMID: 36272649, PMCID: PMC9676401, DOI: 10.1016/j.jbc.2022.102617.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseP38 mitogen-activated protein kinaseMAPK bindingRegulatory mechanismsAllosteric siteMKP family membersNovel allosteric siteSmall molecule targetingMAPK/JNKAdditional regulatory mechanismsPhosphatase functionPhosphatase domainP38 MAPK/JNKProtein kinaseMKP7Site mutantsMAPK signalingAllosteric pocketMolecule targetingMAPK dephosphorylationMutantsNovel siteJNKCatalytic siteDephosphorylationHow to correct relative voxel scale factors for calculations of vector-difference Fourier maps in cryo-EM
Wang J, Liu J, Gisriel CJ, Wu S, Maschietto F, Flesher DA, Lolis E, Lisi GP, Brudvig GW, Xiong Y, Batista VS. How to correct relative voxel scale factors for calculations of vector-difference Fourier maps in cryo-EM. Journal Of Structural Biology 2022, 214: 107902. PMID: 36202310, PMCID: PMC10226527, DOI: 10.1016/j.jsb.2022.107902.Peer-Reviewed Original ResearchConceptsCryo-EM mapsAmino acid residuesAcid residuesCryo-electron microscopy mapIndividual amino acid residuesCyanobacteria Synechocystis spPCC 6803Synechocystis spMicroscopy mapsThermosynechococcus elongatusSARS-CoV-2 spike proteinLocal structural changesResiduesSpike proteinAtomic coordinatesElongatusSubunitsSpeciesProteinSpSimilar structureStructural changesInsights into Binding of Single-Stranded Viral RNA Template to the Replication–Transcription Complex of SARS-CoV‑2 for the Priming Reaction from Molecular Dynamics Simulations
Wang J, Shi Y, Reiss K, Allen B, Maschietto F, Lolis E, Konigsberg WH, Lisi GP, Batista VS. Insights into Binding of Single-Stranded Viral RNA Template to the Replication–Transcription Complex of SARS-CoV‑2 for the Priming Reaction from Molecular Dynamics Simulations. Biochemistry 2022, 61: 424-432. PMID: 35199520, PMCID: PMC8887646, DOI: 10.1021/acs.biochem.1c00755.Peer-Reviewed Original ResearchConceptsReplication-transcription complexPriming reactionRNA duplexesTemplate strandRNA templateHigher-order oligomerizationRNA-dependent RNA polymeraseCryo-EM structureRNA primaseViral RNA templateRNA polymerasePrimer synthesisViral transcriptionSecondary structureViral genomeSubunitsMolecular dynamics simulations
2018
Nanosecond Dynamics Regulate the MIF‐Induced Activity of CD74
Pantouris G, Ho J, Shah D, Syed MA, Leng L, Bhandari V, Bucala R, Batista VS, Loria JP, Lolis E. Nanosecond Dynamics Regulate the MIF‐Induced Activity of CD74. Angewandte Chemie International Edition 2018, 57: 7116-7119. PMID: 29669180, PMCID: PMC6282165, DOI: 10.1002/anie.201803191.Peer-Reviewed Original Research
2016
Macrophage Migration Inhibitory Factor-CXCR4 Receptor Interactions*
Rajasekaran D, Gröning S, Schmitz C, Zierow S, Drucker N, Bakou M, Kohl K, Mertens A, Lue H, Weber C, Xiao A, Luker G, Kapurniotu A, Lolis E, Bernhagen J. Macrophage Migration Inhibitory Factor-CXCR4 Receptor Interactions*. Journal Of Biological Chemistry 2016, 291: 15881-15895. PMID: 27226569, PMCID: PMC4957068, DOI: 10.1074/jbc.m116.717751.Peer-Reviewed Original ResearchConceptsMacrophage migration inhibitory factorChemokine receptorsCXCR4 receptorRole of MIFMIF's biological activityMigration inhibitory factorChemokine receptor interactionsFunctional CXCR4 receptorsClassical chemokine receptorsChemokine-like activityPartial allosteric agonistRegions of CXCR4Inflammatory cytokinesReceptor CD74Leukocyte recruitmentAllosteric agonistInhibitory factorCXCR4Non-cognate interactionsReceptorsPharmacological reagentsReceptor interactionArray analysisGenetic strainsCritical biological responses
2001
Glucocorticoid counter regulation: macrophage migration inhibitory factor as a target for drug discovery
Lolis E. Glucocorticoid counter regulation: macrophage migration inhibitory factor as a target for drug discovery. Current Opinion In Pharmacology 2001, 1: 662-668. PMID: 11757824, DOI: 10.1016/s1471-4892(01)00112-6.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCOP9 Signalosome ComplexDNA-Binding ProteinsDrug DesignGenes, p53GlucocorticoidsHumansInflammationInflammation MediatorsIntracellular Signaling Peptides and ProteinsMacrophage Migration-Inhibitory FactorsMembrane ProteinsMolecular Sequence DataNeoplasmsNeovascularization, PathologicPeptide HydrolasesPhosphoproteinsStructure-Activity RelationshipTranscription FactorsConceptsMacrophage migration inhibitory factorMigration inhibitory factorContribution of MIFInhibitory factorElevated MIF levelsMIF's biological activityActivity of CD4Natural killer cellsInflammatory neurological diseasesInflammatory lung diseasesMIF levelsUlcerative colitisKiller cellsRheumatoid arthritisLung diseaseInflammatory diseasesT cellsHuman studiesNeurological diseasesTherapeutic interventionsDiseaseEndothelial cellsNumber of diseasesIntracellular regulatory proteinsCancerDevelopment of chronic colitis is dependent on the cytokine MIF
de Jong Y, Abadia-Molina A, Satoskar A, Clarke K, Rietdijk S, Faubion W, Mizoguchi E, Metz C, Sahli M, ten Hove T, Keates A, Lubetsky J, Farrell R, Michetti P, van Deventer S, Lolis E, David J, Bhan A, Terhorst C. Development of chronic colitis is dependent on the cytokine MIF. Nature Immunology 2001, 2: 1061-1066. PMID: 11668338, DOI: 10.1038/ni720.Peer-Reviewed Original ResearchMeSH KeywordsAdoptive TransferAnimalsAutoimmune DiseasesBone Marrow TransplantationChronic DiseaseColitisCrohn DiseaseDNA-Binding ProteinsFemaleHumansImmunization, PassiveLipopolysaccharidesMacrophage ActivationMacrophage Migration-Inhibitory FactorsMaleMiceMice, KnockoutModels, AnimalNuclear ProteinsRadiation ChimeraWeight LossConceptsMacrophage migration inhibitory factorCytokine macrophage migration inhibitory factorMIF-deficient miceCrohn's diseaseRole of MIFImmune systemPlasma MIF concentrationMucosal immune systemInnate immune cellsInnate immune systemChronic colitisMIF concentrationsExperimental colitisMIF productionMurine colitisImmune cellsColitisIntestinal bacteriaInhibitory factorDiseaseNew targetsMiceLipopolysaccharideCell typesPatients
2000
Comparison of the Structure of vMIP-II with Eotaxin-1, RANTES, and MCP-3 Suggests a Unique Mechanism for CCR3 Activation † , ‡
Fernandez E, Wilken J, Thompson D, Peiper S, Lolis E. Comparison of the Structure of vMIP-II with Eotaxin-1, RANTES, and MCP-3 Suggests a Unique Mechanism for CCR3 Activation † , ‡. Biochemistry 2000, 39: 12837-12844. PMID: 11041848, DOI: 10.1021/bi001166f.Peer-Reviewed Original ResearchAmino Acid SequenceAnti-HIV AgentsChemokine CCL11Chemokine CCL5Chemokine CCL7ChemokinesChemokines, CCChemotactic Factors, EosinophilCrystallography, X-RayCytokinesHerpesvirus 8, HumanHumansModels, MolecularMolecular Sequence DataMonocyte Chemoattractant ProteinsReceptors, CCR3Receptors, ChemokineReceptors, VirusSequence AlignmentSequence Homology, Amino AcidExpression and coreceptor activity of STRL33/Bonzo on primary peripheral blood lymphocytes.
Sharron M, Pöhlmann S, Price K, Lolis E, Tsang M, Kirchhoff F, Doms R, Lee B. Expression and coreceptor activity of STRL33/Bonzo on primary peripheral blood lymphocytes. Blood 2000, 96: 41-9. PMID: 10891428, DOI: 10.1182/blood.v96.1.41.013k53_41_49.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDB-LymphocytesCell LineCells, CulturedFlow CytometryGenes, ReporterGenetic VectorsGreen Fluorescent ProteinsHumansKiller Cells, NaturalLuminescent ProteinsMacaca mulattaReceptors, CCR5Receptors, ChemokineReceptors, CXCR6Receptors, CytokineReceptors, G-Protein-CoupledReceptors, VirusTransfectionConceptsPeripheral blood lymphocytesPeripheral blood mononuclear cellsSimian immunodeficiency virusCoreceptor activityRelevant coreceptorAlternative coreceptorsBlood lymphocytesHuman immunodeficiency virus-1 (HIV-1) infectionMost simian immunodeficiency virusesPrimary peripheral blood lymphocytesHuman peripheral blood lymphocytesTumor-infiltrating lymphocytesNatural killer cellsBlood mononuclear cellsVirus-1 infectionPotent CXCR4 antagonistSIV Env proteinsMacaque systemKiller cellsImmunodeficiency virusMononuclear cellsMajor coreceptorMaternal isolatesSIV envelopeSTRL33
1999
Pro-1 of Macrophage Migration Inhibitory Factor Functions as a Catalytic Base in the Phenylpyruvate Tautomerase Activity † , ‡
Lubetsky J, Swope M, Dealwis C, Blake P, Lolis E. Pro-1 of Macrophage Migration Inhibitory Factor Functions as a Catalytic Base in the Phenylpyruvate Tautomerase Activity † , ‡. Biochemistry 1999, 38: 7346-7354. PMID: 10353846, DOI: 10.1021/bi990306m.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAnimalsBinding SitesCatalysisCrystallography, X-RayEnzyme ActivationGlycineHumansHydrogen-Ion ConcentrationIntramolecular OxidoreductasesMacromolecular SubstancesMacrophage Migration-Inhibitory FactorsMethionineMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPhenylpyruvic AcidsProlineRecombinant ProteinsConceptsMacrophage migration inhibitory factorMacrophage migration inhibitory factor (MIF) functionsAnti-inflammatory effectsMigration inhibitory factorImportant immunoregulatory moleculeTautomerase activityImmunoregulatory moleculesPhenylpyruvate tautomerase activityInhibitory factorP-hydroxyphenylpyruvateGlucocorticoidsPro-1CytokinesActivityMacrophage migration inhibitory factor: Cytokine, hormone, or enzyme?
Swope M, Lolis E. Macrophage migration inhibitory factor: Cytokine, hormone, or enzyme? 1999, 139: 1-32. PMID: 10453691, DOI: 10.1007/bfb0033647.Peer-Reviewed Original Research
1998
Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II
Shao W, Fernandez E, Wilken J, Thompson D, Siani M, West J, Lolis E, Schweitzer B. Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II. FEBS Letters 1998, 441: 77-82. PMID: 9877169, DOI: 10.1016/s0014-5793(98)01520-8.Peer-Reviewed Original ResearchConceptsTotal chemical synthesisNuclear magnetic resonanceChemical synthesisX-ray crystallographyThree-dimensional structureStructural studiesSynthesisSecondary structureGenome programNew proteinsMagnetic resonanceSelenomethionine proteinsRecombinant proteinsProtein IIHeavy-atom derivativesProteinMIP IICrystallographyMonomersStructureDeterminationDerivativesCloningHigh resolutionResonanceDirect link between cytokine activity and a catalytic site for macrophage migration inhibitory factor
Swope M, Sun H, Blake P, Lolis E. Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor. The EMBO Journal 1998, 17: 3534-3541. PMID: 9649424, PMCID: PMC1170690, DOI: 10.1093/emboj/17.13.3534.Peer-Reviewed Original ResearchConceptsN-terminal prolineN-terminal regionStructure-based inhibitorsMultiple sequence alignmentThree-dimensional structureInvariant residuesEntire polypeptideMicrobial enzymesCatalytic basePro-1Sequence alignmentMIF homologuesCytokine activityHuman macrophage migration inhibitory factorCatalytic siteProlineInhibitory factorHomologuesUnderlying biological activityP-hydroxyphenylpyruvateProteinMacrophage migration inhibitory factorActive siteBiological activityCrystal structure of chemically synthesized [N33A] stromal cell-derived factor 1α, a potent ligand for the HIV-1 “fusin” coreceptor
Dealwis C, Fernandez E, Thompson D, Simon R, Siani M, Lolis E. Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1α, a potent ligand for the HIV-1 “fusin” coreceptor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 6941-6946. PMID: 9618518, PMCID: PMC22694, DOI: 10.1073/pnas.95.12.6941.Peer-Reviewed Original ResearchMacrophage Migration Inhibitory Factor Interactions with Glutathione and S -Hexylglutathione*
Swope M, Sun H, Klockow B, Blake P, Lolis E. Macrophage Migration Inhibitory Factor Interactions with Glutathione and S -Hexylglutathione*. Journal Of Biological Chemistry 1998, 273: 14877-14884. PMID: 9614090, DOI: 10.1074/jbc.273.24.14877.Peer-Reviewed Original ResearchBinding SitesCircular DichroismEnzyme InhibitorsFluorescenceGlutathioneHumansHydrogen-Ion ConcentrationIntramolecular OxidoreductasesMacrophage Migration-Inhibitory FactorsMagnetic Resonance SpectroscopyModels, MolecularProtein BindingProtein ConformationProtein FoldingRecombinant ProteinsSulfhydryl Compounds
1997
Functional and receptor binding characterization of recombinant murine macrophage inflammatory protein 2: Sequence analysis and mutagenesis identify receptor binding epitopes
Jerva L, Lolis E, Sullivan G. Functional and receptor binding characterization of recombinant murine macrophage inflammatory protein 2: Sequence analysis and mutagenesis identify receptor binding epitopes. Protein Science 1997, 6: 1643-1652. PMID: 9260277, PMCID: PMC2143775, DOI: 10.1002/pro.5560060805.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntigens, CDBase SequenceCell LineChemokine CXCL2Chemokines, CXCCloning, MolecularDNA PrimersEpitopesHumansIntercellular Signaling Peptides and ProteinsMiceMolecular Sequence DataMonokinesMutagenesis, Site-DirectedNeutrophilsReceptors, InterleukinReceptors, Interleukin-8ARecombinant ProteinsSequence Homology, Amino Acid
1996
The subunit structure of human macrophage migration inhibitory factor: evidence for a trimer
Sun H, Swope M, Craig C, Bedarkar S, Bernhagen J, Bucala R, Lolis E. The subunit structure of human macrophage migration inhibitory factor: evidence for a trimer. Protein Engineering Design And Selection 1996, 9: 631-635. PMID: 8875640, DOI: 10.1093/protein/9.8.631.Peer-Reviewed Original Research