Reetika Chaurasia
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Postdoctoral Associate
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Research at a Glance
Yale Co-Authors
Frequent collaborators of Reetika Chaurasia's published research.
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A big-picture view of Reetika Chaurasia's research output by year.
Joseph Vinetz, MD, FACP, FIDSA, FASTMH, BS
Choukri Ben Mamoun, PhD
Erol Fikrig, MD
Gary Désir, MD
Noah Wolcott Palm, PhD
Yingjun Cui, PhD
13Publications
65Citations
Publications
2024
Computational reassessment of RNA-seq data reveals key genes in active tuberculosis
Arya R, Shakya H, Chaurasia R, Kumar S, Vinetz J, Kim J. Computational reassessment of RNA-seq data reveals key genes in active tuberculosis. PLOS ONE 2024, 19: e0305582. PMID: 38935691, PMCID: PMC11210783, DOI: 10.1371/journal.pone.0305582.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsConceptsMolecular Complex DetectionProtein-protein interactionsDeregulated genesGene OntologyRNA-seq dataGene Expression Omnibus (GEO) databaseIncreasing prevalence of multidrug-resistantGEO2R online toolPrevalence of multidrug resistancePathway enrichment analysisExpression levelsPatterns of variationGene expression levelsArea under curveInnate immune responseGene networksCore genesMicroarray datasetsSTRING databaseTranscript levelsEnrichment analysisGenesInterferon signalingInterferon-gamma signalingResponse to Mtb infectionAn atlas of human vector-borne microbe interactions reveals pathogenicity mechanisms
Hart T, Sonnert N, Tang X, Chaurasia R, Allen P, Hunt J, Read C, Johnson E, Arora G, Dai Y, Cui Y, Chuang Y, Yu Q, Rahman M, Mendes M, Rolandelli A, Singh P, Tripathi A, Ben Mamoun C, Caimano M, Radolf J, Lin Y, Fingerle V, Margos G, Pal U, Johnson R, Pedra J, Azad A, Salje J, Dimopoulos G, Vinetz J, Carlyon J, Palm N, Fikrig E, Ring A. An atlas of human vector-borne microbe interactions reveals pathogenicity mechanisms. Cell 2024 PMID: 38876107, DOI: 10.1016/j.cell.2024.05.023.Peer-Reviewed Original ResearchAltmetricConceptsCell invasionHost-microbe interactionsArthropod-borne pathogensHost sensingMicrobe interactionsTranscriptional regulationLyme disease spirocheteMicrobial interactionsExtracellular proteinsMicrobial pathogenesisEpidermal growth factorTissue colonizationEnvironmental cuesBacterial selectivityIntracellular pathogensPutative interactionsNext-generation therapeuticsPathogensFunctional investigationsInteractomeVector-borne diseasesImmune evasionPathogenic mechanismsStrainUnmet medical needExploring the Role of Extracellular Vesicles in the Pathogenesis of Tuberculosis
Arya R, Shakya H, Chaurasia R, Haque A, Kim J. Exploring the Role of Extracellular Vesicles in the Pathogenesis of Tuberculosis. Genes 2024, 15: 434. PMID: 38674369, PMCID: PMC11049626, DOI: 10.3390/genes15040434.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsConceptsProtein-protein interaction networkRNA-seq datasetsExtracellular vesiclesTB patientsHealthy controlsResponse regulatorCellular processesInteraction networkPathogenesis of tuberculosisExosome biogenesisImmune response regulationImmune cell profilesDEGsPotential biomarkersVAMP5Immune cell infiltration analysisGenesTherapeutic targetImmune cellsGlobal health concernDiagnostic performanceVesiclesDisease progressionTreatment outcomesAccurate diagnosis
2023
Production and Purification of Cysteine-Rich Leptospiral Virulence-Modifying Proteins with or Without mCherry Fusion
Chaurasia R, Liang C, How K, Vieira D, Vinetz J. Production and Purification of Cysteine-Rich Leptospiral Virulence-Modifying Proteins with or Without mCherry Fusion. The Protein Journal 2023, 42: 792-801. PMID: 37653175, DOI: 10.1007/s10930-023-10152-2.Peer-Reviewed Original ResearchConceptsMCherry fusion proteinsFusion proteinMCherry tagGene familyMCherry fusionsProtein productionFluorescent fusion proteinsRecombinant protein expressionRecombinant protein productionVM proteinsSuch proteinsFunctional proteinsCell biologyLike domainFast protein liquid chromatographyLeptospiral virulenceSoluble proteinUnique memberPink coloniesProtein scienceStructural predictionsProtein liquid chromatographyRicin BFunctional studiesProteinIn silico prediction of molecular mechanisms of toxicity mediated by the leptospiral PF07598 gene family-encoded virulence-modifying proteins
Chaurasia R, Vinetz J. In silico prediction of molecular mechanisms of toxicity mediated by the leptospiral PF07598 gene family-encoded virulence-modifying proteins. Frontiers In Molecular Biosciences 2023, 9: 1092197. PMID: 36756251, PMCID: PMC9900628, DOI: 10.3389/fmolb.2022.1092197.Peer-Reviewed Original ResearchCitationsAltmetricConceptsMolecular dynamics simulationsProtein structure-function relationshipsSecondary structure contentDynamics simulationsVM proteinsStructure-function relationshipsStructure-function studiesStructure contentDivalent cationsSurface bindingRicin BMechanistic understandingBinding residuesC-terminal similaritySilico predictionCationsIonsRicin toxinLeptospirosis pathogenesisDNase I.AB toxins
2022
Comparison of the PF07598-Encoded Virulence-Modifying Proteins of L. interrogans and L. borgpetersenii
Vieira D, Chaurasia R, Vinetz J. Comparison of the PF07598-Encoded Virulence-Modifying Proteins of L. interrogans and L. borgpetersenii. Tropical Medicine And Infectious Disease 2022, 8: 14. PMID: 36668921, PMCID: PMC9863803, DOI: 10.3390/tropicalmed8010014.Peer-Reviewed Original ResearchCitationsConceptsVM proteinsEukaryotic cellsGene familyEnvironmental nichesDifferent cladesMammalian hostsSeverity of outbreaksVirulence effectsCellular pathogenesisHuman pathogensMediated TransmissionLeptospiral speciesParalogsPathogenic groupsProteinVaccine-mediated preventionSpeciesL. interrogansL. borgpeterseniiProtein exotoxinsNew strainFatal leptospirosisTarget cellsLeptospirosis pathogenesisInfectious diseasesVaccination With Leptospira interrogans PF07598 Gene Family-Encoded Virulence Modifying Proteins Protects Mice From Severe Leptospirosis and Reduces Bacterial Load in the Liver and Kidney
Chaurasia R, Salovey A, Guo X, Desir G, Vinetz JM. Vaccination With Leptospira interrogans PF07598 Gene Family-Encoded Virulence Modifying Proteins Protects Mice From Severe Leptospirosis and Reduces Bacterial Load in the Liver and Kidney. Frontiers In Cellular And Infection Microbiology 2022, 12: 926994. PMID: 35837473, PMCID: PMC9274288, DOI: 10.3389/fcimb.2022.926994.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsLethal challenge infectionChallenge infectionBacterial loadC3H/HeJ miceKey target organClinical pathogenesisSevere leptospirosisOrgan infectionProtein immunizationHeJ miceSerovar CanicolaTarget organsAnimal modelsLeptospirosis pathogenesisCellular pathogenesisMicePathogenesisInfectionLeptospira interrogansVirulence factorsModifying proteinsImmunizationKidneyLeptospirosisLiverPathogenic Leptospira Evolved a Unique Gene Family Comprised of Ricin B-Like Lectin Domain-Containing Cytotoxins
Chaurasia R, Marroquin AS, Vinetz JM, Matthias MA. Pathogenic Leptospira Evolved a Unique Gene Family Comprised of Ricin B-Like Lectin Domain-Containing Cytotoxins. Frontiers In Microbiology 2022, 13: 859680. PMID: 35422779, PMCID: PMC9002632, DOI: 10.3389/fmicb.2022.859680.Peer-Reviewed Original ResearchCitationsAltmetricConceptsVM proteinsUnique gene familiesStructural homology searchRecombinant ricin B chainΒ-trefoil domainR-type lectinsCaspase-3 activationHeLa cell surfaceBacterial plasmid DNAGene familyImportant virulence determinantN-terminal fragmentHomology searchCell surface bindingRicin B chainHuman cellsNuclear fragmentationB domainHeLa cellsCell surfaceNuclear translocationVirulence determinantsDNase activityDNase functionProtein
2020
Cytotoxicity of the 42 kDa SMase C sphingomyelinase secreted by Leptospira interrogans serovar Pomona on Vero cells.
Chaurasia R, Sritharan M. Cytotoxicity of the 42 kDa SMase C sphingomyelinase secreted by Leptospira interrogans serovar Pomona on Vero cells. Microbiology 2020, 166: 1065-1073. PMID: 32985970, DOI: 10.1099/mic.0.000976.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsVero cellsSerovar PomonaHaemorrhagic manifestationsHost cell damageEarly diagnosisSevere formHuman patientsExperimental animalsLeptospira interrogansLeptospirosisCandidate markersSphingomyelinase activityHaemolytic activityPomonaSphingomyelinasePathogenic membersCytotoxicitySphingomyelinase geneActive formHigh levelsCellsPatientsDiagnosisConfocal imagesSphingomyelinases
2018
Pathogen-specific leptospiral proteins in urine of patients with febrile illness aids in differential diagnosis of leptospirosis from dengue
Chaurasia R, Thresiamma K, Eapen C, Zachariah B, Paul R, Sritharan M. Pathogen-specific leptospiral proteins in urine of patients with febrile illness aids in differential diagnosis of leptospirosis from dengue. European Journal Of Clinical Microbiology & Infectious Diseases 2018, 37: 423-433. PMID: 29332210, DOI: 10.1007/s10096-018-3187-9.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsMicroscopic agglutination testAnti-leptospiral antibodiesEnzyme-linked immunosorbent assayLeptospiral antigensDifferential diagnosisGroup I patientsUrine of patientsPUO patientsI patientsUrinary antigenClinical symptomsDengue patientsNon-invasive methodStudy groupPatientsHigh titresDengue feverAgglutination testUnknown originInfectious diseasesAntigenDiagnosisImmunosorbent assayUrine samplesSpecific antibodies