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 ResearchMCherry 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 ResearchMolecular 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 ResearchVM proteinsEukaryotic cellsGene familyEnvironmental nichesDifferent cladesMammalian hostsSeverity of outbreaksVirulence effectsCellular pathogenesisHuman pathogensMediated TransmissionLeptospiral speciesParalogsPathogenic groupsProteinVaccine-mediated preventionSpeciesL. interrogansL. borgpeterseniiProtein exotoxinsNew strainFatal leptospirosisTarget cellsLeptospirosis pathogenesisInfectious diseasesPathogenic 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 ResearchVM 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