2020
An Ixodes scapularis Protein Disulfide Isomerase Contributes to Borrelia burgdorferi Colonization of the Vector
Cao Y, Rosen C, Arora G, Gupta A, Booth CJ, Murfin KE, Cerny J, Lopez A, Chuang YM, Tang X, Pal U, Ring A, Narasimhan S, Fikrig E. An Ixodes scapularis Protein Disulfide Isomerase Contributes to Borrelia burgdorferi Colonization of the Vector. Infection And Immunity 2020, 88: 10.1128/iai.00426-20. PMID: 32928964, PMCID: PMC7671890, DOI: 10.1128/iai.00426-20.Peer-Reviewed Original ResearchConceptsTick gutTick bite siteVector-host interfaceAbility of spirochetesProtein disulfide isomerase A3Infected vertebrate hostsInflammatory responseBite siteLyme diseaseVertebrate hostsGutTick proteinsAdditional targetsMiceSpirochete life cycleSpirochete survivalArthropod vectorsSpirochetesRNA interferenceIllnessTicks
2013
Characterization of Ixophilin, A Thrombin Inhibitor from the Gut of Ixodes scapularis
Narasimhan S, Perez O, Mootien S, DePonte K, Koski RA, Fikrig E, Ledizet M. Characterization of Ixophilin, A Thrombin Inhibitor from the Gut of Ixodes scapularis. PLOS ONE 2013, 8: e68012. PMID: 23874485, PMCID: PMC3706618, DOI: 10.1371/journal.pone.0068012.Peer-Reviewed Original ResearchConceptsTick gutBlood mealVertebrate hostsTick gut proteinsPathogen transmissionBorrelia burgdorferi transmissionAnticoagulation strategiesThrombin inhibitory activityHemostatic mechanismThrombin inhibitorsMammalian coagulationIxodes scapularisMammalian hostsTick salivaLyme diseaseKey enzymeGut proteinsBorrelia burgdorferiTick feedingHost bloodHours of feedingGutFunctional suiteTick proteinsHuman pathogens
2011
A Tick Mannose-Binding Lectin Inhibitor Interferes with the Vertebrate Complement Cascade to Enhance Transmission of the Lyme Disease Agent
Schuijt TJ, Coumou J, Narasimhan S, Dai J, DePonte K, Wouters D, Brouwer M, Oei A, Roelofs JJ, van Dam AP, van der Poll T, Veer C, Hovius JW, Fikrig E. A Tick Mannose-Binding Lectin Inhibitor Interferes with the Vertebrate Complement Cascade to Enhance Transmission of the Lyme Disease Agent. Cell Host & Microbe 2011, 10: 136-146. PMID: 21843870, PMCID: PMC3170916, DOI: 10.1016/j.chom.2011.06.010.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBorrelia burgdorferiCell Migration AssaysCloning, MolecularComplement Membrane Attack ComplexComplement Pathway, Mannose-Binding LectinFemaleGene SilencingHemolysisHumansImmunization, PassiveImmunotherapy, ActiveInsect ProteinsIxodesLarvaLyme DiseaseMiceMice, Inbred C3HMolecular Sequence DataNeutrophilsNymphPhagocytosisRabbitsRecombinant ProteinsSalivaSalivary Proteins and PeptidesSequence AlignmentConceptsComplement cascadeLyme disease agent Borrelia burgdorferiImpaired neutrophil phagocytosisTick salivary proteinsVector-borne pathogensLyme disease agentMammalian infectionVector colonizationVertebrate hostsTick midgutAlternative complement pathwayBorrelia transmissionComplement-mediated killingVector proteinNeutrophil phagocytosisEssential rolePathway inhibitorComplement pathwayDisease agentsSalivary proteinsBorrelia burgdorferiLectin inhibitorsProteinCascadeIxodes ticks
2007
Identification of Salp15 Homologues in Ixodes ricinus Ticks
Hovius JW, Ramamoorthi N, Veer C, de Groot KA, Nijhof AM, Jongejan F, van Dam AP, Fikrig E. Identification of Salp15 Homologues in Ixodes ricinus Ticks. Vector-Borne And Zoonotic Diseases 2007, 7: 296-303. PMID: 17896872, DOI: 10.1089/vbz.2006.0624.Peer-Reviewed Original ResearchConceptsSalp15 homologuesI. scapularis Salp15T cell activationDifferent Ixodes speciesAmino acid sequenceEntire amino acid sequenceSignal sequenceMammalian hostsProtein sequencesAcid sequenceC-terminusReverse transcriptase-polymerase chain reactionSensu strictoIxodes speciesSensu latoMajor vectorHomologuesB. burgdorferi sensu latoBorrelia speciesProteinSalp15Borrelia burgdorferi sensu strictoSpeciesI. ricinusBurgdorferi sensu stricto
2006
The Lyme disease agent Borrelia burgdorferi requires BB0690, a Dps homologue, to persist within ticks
Li X, Pal U, Ramamoorthi N, Liu X, Desrosiers DC, Eggers CH, Anderson JF, Radolf JD, Fikrig E. The Lyme disease agent Borrelia burgdorferi requires BB0690, a Dps homologue, to persist within ticks. Molecular Microbiology 2006, 63: 694-710. PMID: 17181780, DOI: 10.1111/j.1365-2958.2006.05550.x.Peer-Reviewed Original ResearchCrystal Structure of West Nile Virus Envelope Glycoprotein Reveals Viral Surface Epitopes
Kanai R, Kar K, Anthony K, Gould LH, Ledizet M, Fikrig E, Marasco WA, Koski RA, Modis Y. Crystal Structure of West Nile Virus Envelope Glycoprotein Reveals Viral Surface Epitopes. Journal Of Virology 2006, 80: 11000-11008. PMID: 16943291, PMCID: PMC1642136, DOI: 10.1128/jvi.01735-06.Peer-Reviewed Original ResearchConceptsWest Nile virus-specific antibodiesEnvelope glycoproteinTick-borne encephalitis virusWest Nile Virus Envelope GlycoproteinLife-threatening encephalitisVirus-specific antibodiesWest Nile virusMajor envelope glycoproteinAntiviral vaccinesVirus envelope glycoproteinDengue virusEncephalitis virusFlavivirus genusViral attachmentReceptor bindingWest NileTherapeutic antibodiesMolecular landscapeNile virusVirusSurface epitopesE proteinViruses e.Viral surfaceVirus surface
2002
A novel family of anticoagulants from the saliva of Ixodes scapularis
Narasimhan S, Koski RA, Beaulieu B, Anderson JF, Ramamoorthi N, Kantor F, Cappello M, Fikrig E. A novel family of anticoagulants from the saliva of Ixodes scapularis. Insect Molecular Biology 2002, 11: 641-650. PMID: 12421422, DOI: 10.1046/j.1365-2583.2002.00375.x.Peer-Reviewed Original ResearchConceptsN-terminal amino acid sequenceSalivary gland cDNA libraryAmino acid sequenceN-terminal sequenceCDNA libraryAcid sequenceAnticoagulant proteinsIxodes scapularisMolecular approachesTerminal sequenceIntrinsic pathwayEscherichia coliSpecific inhibitorNovel familyProteinSalp14Different functionsTick salivaSequenceBiological activityDose-dependent mannerProtease inhibitorsReversed-phase HPLCParaloguesScapularis
2001
Borrelia burgdorferi-Induced Inflammation Facilitates Spirochete Adaptation and Variable Major Protein-Like Sequence Locus Recombination
Anguita J, Thomas V, Samanta S, Persinski R, Hernanz C, Barthold S, Fikrig E. Borrelia burgdorferi-Induced Inflammation Facilitates Spirochete Adaptation and Variable Major Protein-Like Sequence Locus Recombination. The Journal Of Immunology 2001, 167: 3383-3390. PMID: 11544329, PMCID: PMC4309988, DOI: 10.4049/jimmunol.167.6.3383.Peer-Reviewed Original ResearchMeSH KeywordsAdaptation, PhysiologicalAnimalsAntibodies, BacterialAntigens, BacterialAntigens, SurfaceBacterial ProteinsBase SequenceBorrelia burgdorferiCD4-Positive T-LymphocytesDNA, BacterialGene Expression RegulationImmune SeraImmunocompetenceInflammationInterferon-gammaInterleukin-12LipoproteinsLyme DiseaseMiceMice, Inbred C3HMice, KnockoutMolecular Sequence DataReceptors, InterferonRecombination, GeneticSequence AlignmentSequence Homology, Nucleic AcidConceptsImmunocompetent miceDeficient miceB. burgdorferi N40IFN-gammaRMurine immune responseIFN-gamma-mediated responsesIFN-gamma-mediated signalsSpirochetal burdensSpirochete clearanceIL-12Immune responseIFN-gammaControl animalsDifferential immunoscreeningMice resultsMiceVariable major proteinsRT-PCRVivo adaptationB. burgdorferiClearanceBorrelia burgdorferi gene expressionB. burgdorferi survivalAdministrationVivo
1996
Characterization of a 30-kDa Borrelia burgdorferi substrate-binding protein homologue
Das S, Shraga D, Gannon C, Lam TT, Feng S, Brunet LR, Telford SR, Barthold SW, Flavell RA, Fikrig E. Characterization of a 30-kDa Borrelia burgdorferi substrate-binding protein homologue. Research In Microbiology 1996, 147: 739-751. PMID: 9296108, DOI: 10.1016/s0923-2508(97)85121-2.Peer-Reviewed Original ResearchConceptsSubstrate-binding proteinGram-negative bacteriaPeriplasmic substrate-binding proteinB. burgdorferiProtein homologueOligopeptide permeaseChromosomal genesConsiderable homologyP30 expressionB. burgdorferi-infected miceMolecular massSensu latoAmino acidsC3H/HeN miceLyme diseaseB. burgdorferi sensu latoBurgdorferi-infected miceSubset of patientsP30 geneMurine Lyme borreliosisGenesLate-stage infectionRegion 36Recombinant p30Anti-p30 serum
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