2015
Dengue Virus Infection of Aedes aegypti Requires a Putative Cysteine Rich Venom Protein
Londono-Renteria B, Troupin A, Conway MJ, Vesely D, Ledizet M, Roundy CM, Cloherty E, Jameson S, Vanlandingham D, Higgs S, Fikrig E, Colpitts TM. Dengue Virus Infection of Aedes aegypti Requires a Putative Cysteine Rich Venom Protein. PLOS Pathogens 2015, 11: e1005202. PMID: 26491875, PMCID: PMC4619585, DOI: 10.1371/journal.ppat.1005202.Peer-Reviewed Original ResearchConceptsDENV infectionVirus infectionDengue virusCysteine-rich venom proteinsSpecific antiviral therapyDengue virus infectionMosquito-borne flavivirusAedes aegypti cellsAntiviral therapyFlavivirus infectionMultiple flavivirusesTherapeutic measuresNew treatmentsAedes aegyptiInfectionGene targetsSerious human diseasesAegypti cellsMosquito vectorsVaccineVenom proteinsFlavivirusesHuman diseasesMosquitoesAntiserum inhibits
2013
Plasmodium falciparum phosphoethanolamine methyltransferase is essential for malaria transmission
Bobenchik AM, Witola WH, Augagneur Y, Lochlainn L, Garg A, Pachikara N, Choi JY, Zhao YO, Usmani-Brown S, Lee A, Adjalley SH, Samanta S, Fidock DA, Voelker DR, Fikrig E, Mamoun C. Plasmodium falciparum phosphoethanolamine methyltransferase is essential for malaria transmission. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 18262-18267. PMID: 24145416, PMCID: PMC3831454, DOI: 10.1073/pnas.1313965110.Peer-Reviewed Original ResearchMeSH KeywordsAntimalarialsEnzyme InhibitorsFemaleFluorescent Antibody TechniqueHumansMalaria, FalciparumMaleMethyltransferasesPlasmodium falciparumRadiometryReproduction, AsexualSerineConceptsAsexual replicationGametocyte developmentFunctional complementation assaysPhosphoethanolamine N-methyltransferaseHost serineComplementation assaysMalaria transmissionGenetic diversityPhosphoethanolamine methyltransferaseGametocyte differentiationFemale gametocytesSpecificity of inhibitionMetabolic analysisSynthesis of phosphatidylcholineGametocytogenesisChemical screeningPlasmodium speciesAnopheles mosquitoesN-methyltransferaseLow micromolar rangePathwayReplicationHuman erythrocytesParasitesGlobal burden
2007
Antibodies Targeting Linear Determinants of the Envelope Protein Protect Mice against West Nile Virus
Ledizet M, Kar K, Foellmer HG, Bonafé N, Anthony KG, Gould LH, Bushmich SL, Fikrig E, Koski RA. Antibodies Targeting Linear Determinants of the Envelope Protein Protect Mice against West Nile Virus. The Journal Of Infectious Diseases 2007, 196: 1741-1748. PMID: 18190253, DOI: 10.1086/523654.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodies, ViralAntibody AffinityChlorocebus aethiopsDrosophilaEpitopesFemaleFluorescent Antibody TechniqueHorsesImmunization, PassiveImmunoglobulinsMiceMice, Inbred C3HMolecular Sequence DataPeptide FragmentsVero CellsViral Envelope ProteinsWest Nile FeverWest Nile virusConceptsE proteinMultiple flavivirus infectionsVirus-neutralizing antibodiesE protein epitopesFlavivirus envelope proteinProtect miceWest Nile virusFlavivirus infectionLethal challengeProtective antibodiesWest Nile virus E proteinProtective epitopesVirus E proteinRelated flavivirusesImmunoglobulinAntibodiesNile virusLinear determinantsEpitopesEnvelope proteinProtein epitopesMiceHost cell membraneWNVPeptidesOuter Surface Protein B Is Critical for Borrelia burgdorferi Adherence and Survival within Ixodes Ticks
Neelakanta G, Li X, Pal U, Liu X, Beck DS, DePonte K, Fish D, Kantor FS, Fikrig E. Outer Surface Protein B Is Critical for Borrelia burgdorferi Adherence and Survival within Ixodes Ticks. PLOS Pathogens 2007, 3: e33. PMID: 17352535, PMCID: PMC1817655, DOI: 10.1371/journal.ppat.0030033.Peer-Reviewed Original Research
1997
Borrelia burgdorferi strain-specific Osp C-mediated immunity in mice
Bockenstedt LK, Hodzic E, Feng S, Bourrel KW, de Silva A, Montgomery RR, Fikrig E, Radolf JD, Barthold SW. Borrelia burgdorferi strain-specific Osp C-mediated immunity in mice. Infection And Immunity 1997, 65: 4661-4667. PMID: 9353047, PMCID: PMC175668, DOI: 10.1128/iai.65.11.4661-4667.1997.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, BacterialAntigens, BacterialBacterial Outer Membrane ProteinsBorrelia burgdorferi GroupEpitopesFemaleFluorescent Antibody TechniqueMiceMice, Inbred C3HSpecies SpecificityConceptsChallenge infectionC antiserumImmunization studiesStrain-specific immunityAntibody-mediated immunityPassive immunization studiesImmune mouse serumSurface protein AOuter surface protein ADisease regressionInfected miceBorreliacidal activityC antibodySpirochete Borrelia burgdorferiAnimal modelsImmune serumMouse serumInfectionLyme borreliosisMiceHyperimmune serumOsp AImmunofluorescence studiesBorrelia burgdorferiSurface expression
1996
Borrelia burgdorferi OspA is an arthropod-specific transmission-blocking Lyme disease vaccine.
de Silva AM, Telford SR, Brunet LR, Barthold SW, Fikrig E. Borrelia burgdorferi OspA is an arthropod-specific transmission-blocking Lyme disease vaccine. Journal Of Experimental Medicine 1996, 183: 271-275. PMID: 8551231, PMCID: PMC2192397, DOI: 10.1084/jem.183.1.271.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, BacterialAntigens, BacterialAntigens, SurfaceArachnid VectorsBacterial Outer Membrane ProteinsBacterial VaccinesBorrelia burgdorferi GroupDigestive SystemFluorescent Antibody TechniqueImmunotherapy, AdoptiveIxodesLipoproteinsLyme DiseaseMiceMice, Inbred C3HSalivary GlandsConceptsOspA antibodiesTick attachmentUnfed nymphal ticksLyme disease vaccineB. burgdorferi infectionBlood mealMechanism of protectionTick blood mealSpirochete infectionBurgdorferi infectionDisease vaccineGland invasionExpression of OspAOuter surface proteinsSpirochetal agentLyme diseaseMiceSalivary gland invasionAntibodiesSalivary glandsBorrelia burgdorferiIxodes ticksOspA expressionTick gutVaccine
1994
Outer surface proteins E and F of Borrelia burgdorferi, the agent of Lyme disease
Lam TT, Nguyen TP, Montgomery RR, Kantor FS, Fikrig E, Flavell RA. Outer surface proteins E and F of Borrelia burgdorferi, the agent of Lyme disease. Infection And Immunity 1994, 62: 290-298. PMID: 8262642, PMCID: PMC186099, DOI: 10.1128/iai.62.1.290-298.1994.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsBase SequenceBlotting, WesternBorrelia burgdorferi GroupCloning, MolecularCodonFluorescent Antibody TechniqueGenes, BacterialHumansLipoproteinsLyme DiseaseMolecular Sequence DataMolecular WeightOperonRegulatory Sequences, Nucleic AcidRestriction MappingSequence AlignmentSequence Homology, Nucleic AcidSolubilityConceptsOspE genesMolecular massSignal peptidase IIConsensus cleavage sequenceTranscriptional unitsLeader sequenceCommon promoterBp downstreamOuter surface proteinsProtein EStop codonSurface lipoproteinsLabeling showBorrelia burgdorferiGenesHydrophobic domainCleavage sequenceSurface proteinsAmino acidsPeptidase IIProteinOuter surface protein EGel electrophoresisNucleotidesImmunofluorescence studies
1993
Evasion 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 AHistopathologyInfectionDiseaseImmunity