2024
Salp14 epitope-based mRNA vaccination induces early recognition of a tick bite
Cui Y, Cibichakravarthy B, Tang X, Alameh M, Dwivedi G, Weissman D, Fikrig E. Salp14 epitope-based mRNA vaccination induces early recognition of a tick bite. Vaccine 2024, 42: 126304. PMID: 39236403, PMCID: PMC11416896, DOI: 10.1016/j.vaccine.2024.126304.Peer-Reviewed Original ResearchTick bite siteGuinea pigsMRNA-LNPMRNA vaccinesBite siteImmunized guinea pigsTiters of IgGIxodes scapularis ticksDevelopment of erythemaLipid nanoparticlesSkin of guinea pigsI. scapularisTicksErythemaHistamine activityPigsTick bitesCarboxyl terminusRepeated exposureExposure of animalsAmino acidsSalivary proteinsVaccineMRNAGuinea
2016
A novel mosquito ubiquitin targets viral envelope protein for degradation and reduces virion production during dengue virus infection
Troupin A, Londono-Renteria B, Conway MJ, Cloherty E, Jameson S, Higgs S, Vanlandingham DL, Fikrig E, Colpitts TM. A novel mosquito ubiquitin targets viral envelope protein for degradation and reduces virion production during dengue virus infection. Biochimica Et Biophysica Acta 2016, 1860: 1898-1909. PMID: 27241849, PMCID: PMC4949077, DOI: 10.1016/j.bbagen.2016.05.033.Peer-Reviewed Original ResearchConceptsProtein degradationUbiquitin proteinGene expressionProtein expression constructsSite-directed mutagenesisViral protein degradationInnate immune signalingDengue virusProteasomal degradationProtein interactionsExpression constructsMosquito cellsSignificant human diseaseMicroarray analysisImmune signalingViral envelope proteinsVirus infectionHuman diseasesBlood feedingAmino acidsProteinMultiple functionsQRT-PCRVirion productionAntiviral function
2012
Anaplasma phagocytophilum Asp14 Is an Invasin That Interacts with Mammalian Host Cells via Its C Terminus To Facilitate Infection
Kahlon A, Ojogun N, Ragland SA, Seidman D, Troese MJ, Ottens AK, Mastronunzio JE, Truchan HK, Walker NJ, Borjesson DL, Fikrig E, Carlyon JA. Anaplasma phagocytophilum Asp14 Is an Invasin That Interacts with Mammalian Host Cells via Its C Terminus To Facilitate Infection. Infection And Immunity 2012, 81: 65-79. PMID: 23071137, PMCID: PMC3536139, DOI: 10.1128/iai.00932-12.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnaplasma phagocytophilumAnimalsBacterial Outer Membrane ProteinsBinding SitesCell AdhesionCell Line, TumorEhrlichiaEhrlichiosisGene Expression Regulation, BacterialGlutathione TransferaseHL-60 CellsHumansMembrane GlycoproteinsMembrane ProteinsMiceMolecular Sequence DataProtein BindingProtein Structure, TertiaryProteomeSequence Analysis, ProteinTranscription, GeneticUp-RegulationConceptsMammalian host cellsHost cellsReticulate cellsOuter membrane protein candidatesSurface proteinsOuter membrane protein AMembrane protein AA. phagocytophilum-infected ticksObligate intracellular bacteriumA. phagocytophilumGlutathione S-transferaseTranscriptional profilingSurface proteomeC-terminusAffinity purificationFamily AnaplasmataceaeProtein candidatesSelective biotinylationCellular invasionAsp14Transmission feedingAmino acidsS-transferaseIntracellular bacteriumP-selectin glycoprotein ligand-1
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