2019
Borrelia miyamotoi infection leads to cross-reactive antibodies to the C6 peptide in mice and men
Koetsveld J, Platonov A, Kuleshov K, Wagemakers A, Hoornstra D, Ang W, Szekeres S, van Duijvendijk G, Fikrig E, Embers M, Sprong H, Hovius J. Borrelia miyamotoi infection leads to cross-reactive antibodies to the C6 peptide in mice and men. Clinical Microbiology And Infection 2019, 26: 513.e1-513.e6. PMID: 31404672, DOI: 10.1016/j.cmi.2019.07.026.Peer-Reviewed Original ResearchConceptsCross-reactive antibodiesC6 peptideEnzyme immunoassayLyme borreliosisBorrelia miyamotoi infectionBMD patientsExperimental murine infectionC6 enzyme immunoassayAvailable immunoblotNegative immunoblotMiyamotoi infectionTick bitePatient seraMurine infectionPatientsReactivity testingInfectionVlsE proteinBorrelia miyamotoiBorrelia burgdorferiMice
2013
ELF4 is critical for induction of type I interferon and the host antiviral response
You F, Wang P, Yang L, Yang G, Zhao YO, Qian F, Walker W, Sutton R, Montgomery R, Lin R, Iwasaki A, Fikrig E. ELF4 is critical for induction of type I interferon and the host antiviral response. Nature Immunology 2013, 14: 1237-1246. PMID: 24185615, PMCID: PMC3939855, DOI: 10.1038/ni.2756.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineCells, CulturedDNA-Binding ProteinsHEK293 CellsHeLa CellsHost-Pathogen InteractionsHumansImmunoblottingInterferon Regulatory Factor-3Interferon Regulatory Factor-7Interferon-betaMembrane ProteinsMiceMice, Inbred C57BLMice, KnockoutMicroscopy, ConfocalProtein BindingReverse Transcriptase Polymerase Chain ReactionRNA InterferenceSignal TransductionSurvival AnalysisTranscription FactorsTranscriptional ActivationWest Nile FeverWest Nile virus
2012
Expression of Ixodes scapularis Antifreeze Glycoprotein Enhances Cold Tolerance in Drosophila melanogaster
Neelakanta G, Hudson AM, Sultana H, Cooley L, Fikrig E. Expression of Ixodes scapularis Antifreeze Glycoprotein Enhances Cold Tolerance in Drosophila melanogaster. PLOS ONE 2012, 7: e33447. PMID: 22428051, PMCID: PMC3302814, DOI: 10.1371/journal.pone.0033447.Peer-Reviewed Original ResearchMeSH KeywordsAcclimatizationAnalysis of VarianceAnimalsAnimals, Genetically ModifiedAntifreeze ProteinsApoptosisCold TemperatureDrosophila melanogasterEmbryo, NonmammalianEnzyme-Linked Immunosorbent AssayFemaleImmunoblottingIn Situ Nick-End LabelingIxodesMaleMusclesOligonucleotidesReal-Time Polymerase Chain ReactionConceptsNon-freezing temperaturesD. melanogasterDrosophila melanogasterCold toleranceLow non-freezing temperaturesFemale adult fliesTransgenic D. melanogasterCold shock injuryAbility of fliesAntifreeze glycoproteinsAdult fliesMolecular basisMelanogasterFlight musclesFliesAntifreeze proteinsHatching rateHigher survival rateApoptotic damageGlycoproteinExpressionToleranceEmbryosProteinApoptosis
2008
Anaplasma phagocytophilum Increases Cathepsin L Activity, Thereby Globally Influencing Neutrophil Function
Thomas V, Samanta S, Fikrig E. Anaplasma phagocytophilum Increases Cathepsin L Activity, Thereby Globally Influencing Neutrophil Function. Infection And Immunity 2008, 76: 4905-4912. PMID: 18765732, PMCID: PMC2573316, DOI: 10.1128/iai.00851-08.Peer-Reviewed Original ResearchMeSH KeywordsAnaplasma phagocytophilumCathepsin LCathepsinsCysteine EndopeptidasesEhrlichiosisElectrophoretic Mobility Shift AssayGene Expression Regulation, BacterialHL-60 CellsHomeodomain ProteinsHumansImmunoblottingImmunoprecipitationNeutrophilsNuclear ProteinsRepressor ProteinsReverse Transcriptase Polymerase Chain ReactionTranscription FactorsConceptsA. phagocytophilum infectionPhagocytophilum infectionCathepsin L activityNeutrophil functionA. phagocytophilumL activityHuman neutrophil peptides 1Polymorphonuclear leukocyte functionNeutrophil peptide-1Human granulocytic anaplasmosisTherapeutic optionsNeutrophil defenseLeukocyte functionCathepsin LPeptide-1InfectionObligate intracellular pathogensMarked reductionGranulocytic anaplasmosisIntracellular pathogensCDP activityHost oxidative burstAnaplasma phagocytophilumPhagocytophilumOxidative burst
1999
Serodiagnosis of Human Granulocytic Ehrlichiosis by a Recombinant HGE-44-Based Enzyme-Linked Immunosorbent Assay
Ijdo J, Wu C, Magnarelli L, Fikrig E. Serodiagnosis of Human Granulocytic Ehrlichiosis by a Recombinant HGE-44-Based Enzyme-Linked Immunosorbent Assay. Journal Of Clinical Microbiology 1999, 37: 3540-3544. PMID: 10523549, PMCID: PMC85687, DOI: 10.1128/jcm.37.11.3540-3544.1999.Peer-Reviewed Original ResearchConceptsPolyvalent enzyme-linked immunosorbent assaysEnzyme-linked immunosorbent assayRecombinant enzyme-linked immunosorbent assayIndirect fluorescent-antibody assaySerum samplesPatient serum samplesFluorescent-antibody assayCurrent antibodyNormal serum samplesImmunosorbent assayHuman granulocytic ehrlichiosisHuman monocytic ehrlichiosisSuitable antigenHigh costGranulocytic ehrlichiosisSerologic testing of horses for granulocytic ehrlichiosis, using indirect fluorescent antibody staining and immunoblot analysis.
Magnarelli L, Van Andel A, Ijdo J, Heimer R, Fikrig E. Serologic testing of horses for granulocytic ehrlichiosis, using indirect fluorescent antibody staining and immunoblot analysis. American Journal Of Veterinary Research 1999, 60: 631-5. PMID: 10328436, DOI: 10.2460/ajvr.1999.60.05.631.Peer-Reviewed Original Research
1998
Cloning of the Gene Encoding the 44-Kilodalton Antigen of the Agent of Human Granulocytic Ehrlichiosis and Characterization of the Humoral Response
Ijdo J, Sun W, Zhang Y, Magnarelli L, Fikrig E. Cloning of the Gene Encoding the 44-Kilodalton Antigen of the Agent of Human Granulocytic Ehrlichiosis and Characterization of the Humoral Response. Infection And Immunity 1998, 66: 3264-3269. PMID: 9632594, PMCID: PMC108341, DOI: 10.1128/iai.66.7.3264-3269.1998.Peer-Reviewed Original ResearchConceptsHuman granulocytic ehrlichiosisGranulocytic ehrlichiosisAgent of HGESera of patientsBorrelia burgdorferi infectionMsp-2 genesElicit specific antibodiesHumoral responseBurgdorferi infectionMurine infectionHealthy individualsPatientsSerumSpecific antibodiesHL-60 cellsInfectionAntibodiesEhrlichia chaffeensisAntigenMiceEhrlichiosisGenomic DNA expression libraryMultigene familyGlutathione transferase fusion proteinFusion proteinPrevention of Borrelia burgdorferi transmission in guinea pigs by tick immunity.
Nazario S, Das S, de Silva AM, Deponte K, Marcantonio N, Anderson JF, Fish D, Fikrig E, Kantor FS. Prevention of Borrelia burgdorferi transmission in guinea pigs by tick immunity. American Journal Of Tropical Medicine And Hygiene 1998, 58: 780-5. PMID: 9660463, DOI: 10.4269/ajtmh.1998.58.780.Peer-Reviewed Original ResearchGranulocytic Ehrlichiosis in Tick-Immune Guinea Pigs
Das S, Deponte K, Marcantonio N, Ijdo J, Hodzic E, Katavolos P, Barthold S, Telford S, Kantor F, Fikrig E. Granulocytic Ehrlichiosis in Tick-Immune Guinea Pigs. Infection And Immunity 1998, 66: 1803-1805. PMID: 9529119, PMCID: PMC108126, DOI: 10.1128/iai.66.4.1803-1805.1998.Peer-Reviewed Original ResearchHeat shock protein 70 of the agent of human granulocytic ehrlichiosis binds to Borrelia burgdorferi antibodies.
Ijdo J, Zhang Y, Anderson M, Goldberg D, Fikrig E. Heat shock protein 70 of the agent of human granulocytic ehrlichiosis binds to Borrelia burgdorferi antibodies. MSphere 1998, 5: 118-20. PMID: 9455892, PMCID: PMC121403, DOI: 10.1128/cdli.5.1.118-120.1998.Peer-Reviewed Original ResearchConceptsHuman granulocytic ehrlichiosisEhrlichial antigenHSP-70Borrelia burgdorferi antibodiesSerologic test resultsHeat shock protein 70Shock protein 70Burgdorferi antibodiesPatient seraGranulocytic ehrlichiosisLyme diseaseFirst weekHeat shock proteinsLyme disease spirochetePrior exposureImmunoglobulin GProtein 70Immunoblot analysisAntigenShock proteinsSerumAntibodiesPatientsIllnessIgG
1997
Temporal pattern of Borrelia burgdorferi p21 expression in ticks and the mammalian host.
Das S, Barthold SW, Giles SS, Montgomery RR, Telford SR, Fikrig E. Temporal pattern of Borrelia burgdorferi p21 expression in ticks and the mammalian host. Journal Of Clinical Investigation 1997, 99: 987-995. PMID: 9062357, PMCID: PMC507907, DOI: 10.1172/jci119264.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, BacterialAntigens, BacterialAntigens, SurfaceArthritis, InfectiousBacterial Outer Membrane ProteinsBacterial ProteinsBacterial VaccinesBorrelia burgdorferi GroupElectrophoresis, Gel, Pulsed-FieldEnzyme-Linked Immunosorbent AssayFemaleFlagellinFluorescent Antibody Technique, IndirectGene Expression Regulation, BacterialHumansImmunizationImmunization, PassiveImmunoblottingIxodesLipoproteinsLyme DiseaseMiceMice, Inbred C3HPlasmidsPolymerase Chain ReactionRecombinant ProteinsRNA, MessengerTime FactorsConceptsInfected miceHumoral responseLate-stage Lyme diseaseMarkers of infectionCourse of diseaseMurine Lyme borreliosisB. burgdorferiB. burgdorferi infectionHuman humoral responseIxodes dammini ticksBurgdorferi-infected miceLyme arthritisActive immunizationMammalian hostsPassive transferBurgdorferi infectionC3H miceMurine infectionDay 14P21 antibodyP21 expressionLyme borreliosisLyme diseaseMiceInfection
1995
Selection of variant Borrelia burgdorferi isolates from mice immunized with outer surface protein A or B
Fikrig E, Tao H, Barthold SW, Flavell RA. Selection of variant Borrelia burgdorferi isolates from mice immunized with outer surface protein A or B. Infection And Immunity 1995, 63: 1658-1662. PMID: 7729870, PMCID: PMC173206, DOI: 10.1128/iai.63.5.1658-1662.1995.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, BacterialAntigens, SurfaceBacterial Outer Membrane ProteinsBacterial VaccinesBorrelia burgdorferi GroupCloning, MolecularFemaleGenes, BacterialGenetic VariationImmunoblottingLipoproteinsLyme DiseaseMiceMice, Inbred C3HRecombinant ProteinsSelection, GeneticSequence Analysis, DNAVaccinationConceptsSurface protein AOuter surface protein AProtective immunityProtective antibodiesIncomplete efficacyMiceMonoclonal antibodiesProtein ABorrelia burgdorferiB. burgdorferiAntigenic diversityOspBOspAVivo selective pressureImmunityAntibodiesB. burgdorferi isolatesBurgdorferiChallenge inoculationPoint mutationsMolecular basisVaccineInfection
1994
Sera from Patients with Chronic Lyme Disease Protect Mice from Lyme Borreliosis
Fikrig E, Bockenstedt L, Barthold S, Chen M, Tao H, Salaam P, Telford S, Flavell R. Sera from Patients with Chronic Lyme Disease Protect Mice from Lyme Borreliosis. The Journal Of Infectious Diseases 1994, 169: 568-574. PMID: 8158028, DOI: 10.1093/infdis/169.3.568.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, BacterialAntigens, BacterialAntigens, SurfaceBacterial Outer Membrane ProteinsBacterial VaccinesBorrelia burgdorferi GroupChronic DiseaseFemaleHumansImmunization, PassiveImmunoblottingLipoproteinsLyme DiseaseMiceMice, Inbred C3HPolymerase Chain ReactionPrecipitin TestsConceptsStrong humoral responseLyme diseaseHumoral responseB. burgdorferiLate-stage Lyme diseaseLate Lyme diseaseElicit protective immunityChronic Lyme diseaseStrong antibody reactivityBorrelia burgdorferi challengeSurface protein AMost patientsOuter surface protein AProtective immunityImmune responsePatientsAntibody reactivityHuman antibodiesInfectionLyme borreliosisMiceDiseaseSerumNatural infectionAntibodies
1993
Serologic analysis of dogs, horses, and cottontail rabbits for antibodies to an antigenic flagellar epitope of Borrelia burgdorferi
Fikrig E, Magnarelli LA, Chen M, Anderson JF, Flavell RA. Serologic analysis of dogs, horses, and cottontail rabbits for antibodies to an antigenic flagellar epitope of Borrelia burgdorferi. Journal Of Clinical Microbiology 1993, 31: 2451-2455. PMID: 7691874, PMCID: PMC265777, DOI: 10.1128/jcm.31.9.2451-2455.1993.Peer-Reviewed Original ResearchSerologic response to the Borrelia burgdorferi flagellin demonstrates an epitope common to a neuroblastoma cell line.
Fikrig E, Berland R, Chen M, Williams S, Sigal LH, Flavell RA. Serologic response to the Borrelia burgdorferi flagellin demonstrates an epitope common to a neuroblastoma cell line. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 183-187. PMID: 7678336, PMCID: PMC45624, DOI: 10.1073/pnas.90.1.183.Peer-Reviewed Original ResearchConceptsNeuroblastoma cell linesHuman neuroblastoma cell linePatient seraCell linesPathogenesis of neuroborreliosisNeural tissueB. burgdorferi flagellinB-cell epitopesAmino acids 213Neurologic manifestationsSerologic responseSpecific B-cell epitopesBorrelia burgdorferi flagellinImmune responseLyme borreliosisMonoclonal antibodiesRecombinant fusion proteinSerumAntibodiesBorrelia burgdorferiEpitopesEpitope mappingFlagellinTissueNeuroborreliosis
1992
Serologic Diagnosis of Lyme Disease using Recombinant Outer Surface Proteins A and Band Flagellin
Fikrig E, Huguenel E, Berland R, Rahn D, Hardin J, Flavell R. Serologic Diagnosis of Lyme Disease using Recombinant Outer Surface Proteins A and Band Flagellin. The Journal Of Infectious Diseases 1992, 165: 1127-1132. PMID: 1583333, DOI: 10.1093/infdis/165.6.1127.Peer-Reviewed Original ResearchConceptsLyme diseaseRecombinant outer surface proteinRecombinant outer surface protein AB. burgdorferi antigensSurface protein AOuter surface protein AEarly diseaseLate diseaseSerologic diagnosisDiagnostic testingOuter surface proteinsImmunogenic regionPatientsDiseaseBorrelia burgdorferiELISAImmunoblotAntibodiesSurface proteinsFlagellinProtein AAntigenDiagnosis
1991
Protection of Mice from Lyme Borreliosis by Oral Vaccination with Escherichia coli Expressing OspA
Fikrig E, Barthold S, Kantor F, Flavell R. Protection of Mice from Lyme Borreliosis by Oral Vaccination with Escherichia coli Expressing OspA. The Journal Of Infectious Diseases 1991, 164: 1224-1227. PMID: 1955724, DOI: 10.1093/infdis/164.6.1224.Peer-Reviewed Original ResearchConceptsOral vaccinationRecombinant OspARecombinant outer surface protein AProtection of miceSerum IgG antibodiesSurface protein ALast boostOuter surface protein AControl miceChallenge infectionIgG antibodiesIntraperitoneal injectionLive Escherichia coliOral preparationsC3H/Day 10Lyme borreliosisVaccinationMiceInfectionBorrelia burgdorferiOspAAntibodiesProtein AGavage