2009
Fusion Loop Peptide of the West Nile Virus Envelope Protein Is Essential for Pathogenesis and Is Recognized by a Therapeutic Cross-Reactive Human Monoclonal Antibody
Sultana H, Foellmer HG, Neelakanta G, Oliphant T, Engle M, Ledizet M, Krishnan MN, Bonafé N, Anthony KG, Marasco WA, Kaplan P, Montgomery RR, Diamond MS, Koski RA, Fikrig E. Fusion Loop Peptide of the West Nile Virus Envelope Protein Is Essential for Pathogenesis and Is Recognized by a Therapeutic Cross-Reactive Human Monoclonal Antibody. The Journal Of Immunology 2009, 183: 650-660. PMID: 19535627, PMCID: PMC3690769, DOI: 10.4049/jimmunol.0900093.Peer-Reviewed Original ResearchConceptsWest Nile virus envelope proteinWest Nile virusVirus envelope proteinDengue virusCross-reactive human monoclonal antibodiesBlood-brain barrier permeabilityEnvelope proteinWest Nile virus infectionNeutralization escape variantsNile virusWest Nile encephalitisNeutralization escape mutantsHuman monoclonal antibodyFatal neurological diseaseParental West Nile virusFusion loopEscape variantsInflammatory responseBarrier permeabilityLethal encephalitisMAb11Virus infectionHuman mAbsEscape mutantsNeurological diseases
2007
A West Nile Virus Recombinant Protein Vaccine That Coactivates Innate and Adaptive Immunity
Huleatt J, Foellmer H, Hewitt D, Tang J, Desai P, Price A, Jacobs A, Takahashi V, Huang Y, Nakaar V, Alexopoulou L, Fikrig E, Powell T, McDonald W. A West Nile Virus Recombinant Protein Vaccine That Coactivates Innate and Adaptive Immunity. The Journal Of Infectious Diseases 2007, 195: 1607-1617. PMID: 17471430, DOI: 10.1086/517613.Peer-Reviewed Original ResearchConceptsImmune responseAntibody responseImmunoglobulin G antibody responseC3H/HeN miceWest Nile virus vaccineAdaptive immune signalsTLR5-deficient miceAntigen-specific responsesG antibody responseProtective immune responseAdaptive immune responsesToll-like receptorsWNV envelope proteinLethal WNV challengeRecombinant protein vaccineInterleukin-8 productionNeutralized viral infectivityEnzyme-linked immunosorbentEffective WNV vaccinesWNV vaccineHeN miceVirus challengeProtein vaccineVirus vaccineWNV challenge
2005
Protective and Therapeutic Capacity of Human Single-Chain Fv-Fc Fusion Proteins against West Nile Virus
Gould LH, Sui J, Foellmer H, Oliphant T, Wang T, Ledizet M, Murakami A, Noonan K, Lambeth C, Kar K, Anderson JF, de Silva AM, Diamond MS, Koski RA, Marasco WA, Fikrig E. Protective and Therapeutic Capacity of Human Single-Chain Fv-Fc Fusion Proteins against West Nile Virus. Journal Of Virology 2005, 79: 14606-14613. PMID: 16282460, PMCID: PMC1287547, DOI: 10.1128/jvi.79.23.14606-14613.2005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, ViralAntibody SpecificityHumansImmunoglobulin Fc FragmentsImmunoglobulin FragmentsMiceRecombinant Fusion ProteinsViral VaccinesWest Nile FeverWest Nile virusConceptsWest Nile virus infectionWest Nile virusVirus infectionNile virusLethal West Nile virus infectionFc fusion proteinEnvelope proteinShort-term prophylaxisRecombinant human scFvsHuman single-chain FvWest Nile virus envelope proteinVariable region antibodiesPassive immunizationFlavivirus infectionVirus envelope proteinHuman vaccinesDay 1Dengue virusHuman scFvRegion antibodiesInfectionTherapeutic capacityMiceSerotype 2Single-chain Fv
2001
Recombinant Protein-44-Based Class-Specific Enzyme-Linked Immunosorbent Assays for Serologic Diagnosis of Human Granulocytic Ehrlichiosis
Magnarelli L, IJdo J, Wu C, Fikrig E. Recombinant Protein-44-Based Class-Specific Enzyme-Linked Immunosorbent Assays for Serologic Diagnosis of Human Granulocytic Ehrlichiosis. European Journal Of Clinical Microbiology & Infectious Diseases 2001, 20: 482-485. PMID: 11561804, DOI: 10.1007/s100960100542.Peer-Reviewed Original ResearchConceptsPolyvalent enzyme-linked immunosorbent assaysClass-specific enzyme-linked immunosorbent assaysEnzyme-linked immunosorbent assayIndirect fluorescent-antibody analysisFluorescent antibody analysisImmunosorbent assaySpecificity testsIgG antibodiesHigh sensitivityHuman granulocytic ehrlichiosisHuman serumGranulocytic ehrlichiosisWhole cell antigenAntibody analysisImmunoglobulin M antibodiesOnset of illnessSerologic diagnosisSerum samplesHuman granulocytic ehrlichiosis (HGE) agentPatient 3False-positive resultsIgM antibodiesM antibodiesTotal immunoglobulinTotal antibody
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 ehrlichiosis
1995
The hook protein of Borrelia burgdorferi, encoded by the flgE gene, is serologically recognized in Lyme disease.
Jwang B, Dewing P, Fikrig E, Flavell RA. The hook protein of Borrelia burgdorferi, encoded by the flgE gene, is serologically recognized in Lyme disease. MSphere 1995, 2: 609-15. PMID: 8548542, PMCID: PMC170207, DOI: 10.1128/cdli.2.5.609-615.1995.Peer-Reviewed Original ResearchConceptsFlgE proteinFlgE geneEscherichia coli expression plasmidPrimary protein sequenceB. burgdorferi N40Hook geneWhole cell lysatesHook proteinLinear chromosomesPeriplasmic flagellaProtein sequencesFlgERecombinant proteinsB. burgdorferiBasal bodiesFlagellar filamentsWestern blot analysisBorrelia burgdorferiGenesExpression plasmidProteinBlot analysisNegative bacteriaMurine antiseraLyme diseaseEfficacy of Human Lyme Disease Vaccine Formulations in a Mouse Model
Telford SR, Kantor FS, Lobet Y, Barthold SW, Spielman A, Flavell RA, Fikrig E. Efficacy of Human Lyme Disease Vaccine Formulations in a Mouse Model. The Journal Of Infectious Diseases 1995, 171: 1368-1370. PMID: 7751719, DOI: 10.1093/infdis/171.5.1368.Peer-Reviewed Original ResearchConceptsMouse modelC3H/HeJ mouse modelLyme diseaseRecombinant outer surface protein APhase I human trialsPhase II trialSurface protein AUnvaccinated miceII trialVaccinated miceOuter surface protein AVaccine formulationsHuman trialsRecombinant OspAMiceBorrelia burgdorferiDiseaseTrialsMajor siteTrial sitesProtein ATicksImmunizationVaccineInfection
1993
Protection against antigenically variable Borrelia burgdorferi conferred by recombinant vaccines.
Telford SR, Fikrig E, Barthold SW, Brunet LR, Spielman A, Flavell RA. Protection against antigenically variable Borrelia burgdorferi conferred by recombinant vaccines. Journal Of Experimental Medicine 1993, 178: 755-758. PMID: 8340764, PMCID: PMC2191140, DOI: 10.1084/jem.178.2.755.Peer-Reviewed Original ResearchInability of truncated recombinant Osp A proteins to elicit protective immunity to Borrelia burgdorferi in mice.
Bockenstedt LK, Fikrig E, Barthold SW, Kantor FS, Flavell RA. Inability of truncated recombinant Osp A proteins to elicit protective immunity to Borrelia burgdorferi in mice. The Journal Of Immunology 1993, 151: 900-6. PMID: 8335917, DOI: 10.4049/jimmunol.151.2.900.Peer-Reviewed Original ResearchConceptsA antibodiesOsp AProtective immunityMurine immune responseBorrelia burgdorferiElicit protective immunityGroups of miceDevelopment of antibodiesOuter surface protein A.Vaccine AgsChallenge infectionPassive immunizationActive immunizationImmune responseEtiologic agentIndirect immunofluorescenceLyme diseaseMiceVaccinationA antiseraAntibodiesImmunityConformational epitopesA proteinImmunizationEvasion of protective immunity by Borrelia burgdorferi by truncation of outer surface protein B.
Fikrig E, Tao H, Kantor FS, Barthold SW, Flavell RA. Evasion of protective immunity by Borrelia burgdorferi by truncation of outer surface protein B. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 4092-4096. PMID: 7683420, PMCID: PMC46452, DOI: 10.1073/pnas.90.9.4092.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodiesAntibodies, MonoclonalAntigens, BacterialAntigens, SurfaceBacterial Outer Membrane ProteinsBase SequenceBorrelia burgdorferi GroupCloning, MolecularCodonEpitopesEscherichia coliFemaleFluorescent Antibody TechniqueGenes, BacterialHumansLyme DiseaseMiceMice, Inbred C3HPolymerase Chain ReactionRecombinant Fusion ProteinsRecombinant ProteinsRestriction MappingTicksVaccines, SyntheticViral VaccinesConceptsProtective immune responseVaccination immunityProtective immunityProtective antibodiesAntibody responseImmune destructionImmune responseHost defenseOuter surface proteinsLyme diseaseOuter surface protein BBorrelia burgdorferiCausative agentOspBMicePolyclonal antibodiesImmunityAntibodiesPresent studyStrain B31Surface proteinsProtein BPrevious studiesVaccinationOspB.Serologic 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
Elimination of Borrelia burgdorferi from vector ticks feeding on OspA-immunized mice.
Fikrig E, Telford SR, Barthold SW, Kantor FS, Spielman A, Flavell RA. Elimination of Borrelia burgdorferi from vector ticks feeding on OspA-immunized mice. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 5418-5421. PMID: 1608951, PMCID: PMC49303, DOI: 10.1073/pnas.89.12.5418.Peer-Reviewed Original ResearchConceptsRecombinant outer surface protein AVaccine-induced immunityIxodes dammini ticksSurface protein AOuter surface protein ANonimmunized miceImmunized miceSpirochetal infectionTick biteCharacteristic histopathologyImmunized animalsLyme diseaseMiceBorrelia burgdorferiSpirochetesMode of protectionVector ticksOspATicksProtein AHistopathologyInfectionDiseaseImmunitySerologic 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
Molecular characterization of the humoral response to the 41-kilodalton flagellar antigen of Borrelia burgdorferi, the Lyme disease agent
Berland R, Fikrig E, Rahn D, Hardin J, Flavell RA. Molecular characterization of the humoral response to the 41-kilodalton flagellar antigen of Borrelia burgdorferi, the Lyme disease agent. Infection And Immunity 1991, 59: 3531-3535. PMID: 1894359, PMCID: PMC258917, DOI: 10.1128/iai.59.10.3531-3535.1991.Peer-Reviewed Original ResearchConceptsLyme diseaseHumoral responseLate-stage Lyme diseaseEarly humoral responseBorrelia burgdorferiFlagellar antigensPolymerase chain reactionSerological testingImmunodominant domainWestern blotPatientsLyme disease agentAntigenDiseaseChain reactionGlutathione S-transferaseFusion proteinAffinity-purified fusion proteinFlagellin fragmentBacterial flagellinSerumBurgdorferiS-transferaseDisease agentsMolecular characterization
1990
Protection of Mice Against the Lyme Disease Agent by Immunizing with Recombinant OspA
Fikrig E, Barthold S, Kantor F, Flavell R. Protection of Mice Against the Lyme Disease Agent by Immunizing with Recombinant OspA. Science 1990, 250: 553-556. PMID: 2237407, DOI: 10.1126/science.2237407.Peer-Reviewed Original ResearchConceptsRecombinant OspALyme borreliosisC3H/HeJ miceProtection of miceTick-borne illnessB. burgdorferi strain N40Recombinant OspA proteinSurface protein AOuter surface protein AHeJ miceLyme disease agentStrain N40Borrelia burgdorferiB. burgdorferiMiceOspABorreliosisOspA proteinBurgdorferiDisease agentsProtein AVaccineIllnessAntibodies