Featured Publications
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
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 ResearchConceptsLethal challenge infectionChallenge infectionBacterial loadC3H/HeJ miceKey target organClinical pathogenesisSevere leptospirosisOrgan infectionProtein immunizationHeJ miceSerovar CanicolaTarget organsAnimal modelsLeptospirosis pathogenesisCellular pathogenesisMicePathogenesisInfectionLeptospira interrogansVirulence factorsModifying proteinsImmunizationKidneyLeptospirosisLiver
2010
Apical Surface Expression of Aspartic Protease Plasmepsin 4, a Potential Transmission-blocking Target of the Plasmodium Ookinete*
Li F, Patra KP, Yowell CA, Dame JB, Chin K, Vinetz JM. Apical Surface Expression of Aspartic Protease Plasmepsin 4, a Potential Transmission-blocking Target of the Plasmodium Ookinete*. Journal Of Biological Chemistry 2010, 285: 8076-8083. PMID: 20056606, PMCID: PMC2832958, DOI: 10.1074/jbc.m109.063388.Peer-Reviewed Original ResearchConceptsPlasmepsin 4Midgut invasionAspartic proteasesDigestive vacuoleMidgut peritrophic matrixApical surface expressionChitin-binding proteinsMass spectrometry sequencingMalaria parasitesPeritrophic matrixPlasmodium invasionAspartic protease inhibitorsPlasmodium ookinetesParasite infectivityApical surfaceDefinitive hostsMechanistic roleAffinity columnBlood-stage PlasmodiumSurface expressionCalpain inhibitorsMidgut basal laminaProteinVaccine targetsVacuoles
2004
Plasmodium Ookinete-secreted Proteins Secreted through a Common Micronemal Pathway Are Targets of Blocking Malaria Transmission*
Li F, Templeton TJ, Popov V, Comer JE, Tsuboi T, Torii M, Vinetz JM. Plasmodium Ookinete-secreted Proteins Secreted through a Common Micronemal Pathway Are Targets of Blocking Malaria Transmission*. Journal Of Biological Chemistry 2004, 279: 26635-26644. PMID: 15069061, DOI: 10.1074/jbc.m401385200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBlotting, WesternCell MembraneChitinasesCulicidaeCytoplasmDNA, ComplementaryElectrophoresis, Polyacrylamide GelEnzyme-Linked Immunosorbent AssayFluorescent Antibody Technique, IndirectImmunohistochemistryLigandsMalariaMicroscopy, ElectronMicroscopy, FluorescenceMicroscopy, ImmunoelectronMolecular Sequence DataPlasmodiumPlasmodium falciparumProtein BindingProtozoan ProteinsReceptors, Cell SurfaceRecombinant ProteinsSequence Homology, Amino AcidSpecies SpecificityConceptsMicroneme secretory organellesDomain-related proteinP. gallinaceumImmunofluorescence localization studiesMicronemal proteinsIndirect immunofluorescence localization studiesSecretory organellesOokinete stagePlasmodium ookinetesLocalization studiesSporogonic stagesParasite infectivityTransmission-blocking vaccine candidateProteinMalaria parasitesPgCHT1Malaria transmission-blocking vaccine candidateApical endA. aegyptiAnopheles mosquitoesAedes aegyptiPlasmodium gallinaceumVon Willebrand factorImmunological targetsVaccine candidates
2001
Leishmania donovani: Expression and Characterization of Escherichia coli-Expressed Recombinant Chitinase LdCHT1
Razek-Desouky A, Specht C, Soong L, Vinetz J. Leishmania donovani: Expression and Characterization of Escherichia coli-Expressed Recombinant Chitinase LdCHT1. Experimental Parasitology 2001, 99: 220-225. PMID: 11888249, DOI: 10.1006/expr.2001.4665.Peer-Reviewed Original Research
2000
Chitinases of the Avian Malaria Parasite Plasmodium gallinaceum, a Class of Enzymes Necessary for Parasite Invasion of the Mosquito Midgut*
Vinetz J, Valenzuela J, Specht C, Aravind L, Langer R, Ribeiro J, Kaslow D. Chitinases of the Avian Malaria Parasite Plasmodium gallinaceum, a Class of Enzymes Necessary for Parasite Invasion of the Mosquito Midgut*. Journal Of Biological Chemistry 2000, 275: 10331-10341. PMID: 10744721, DOI: 10.1074/jbc.275.14.10331.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsChickensChitinasesConsensus SequenceCulicidaeDigestive SystemEpithelial CellsGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicHumansKineticsMalaria, AvianMolecular Sequence DataPlasmodium gallinaceumRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidConceptsAvian malaria parasite Plasmodium gallinaceumMalaria parasite Plasmodium gallinaceumChitin-containing peritrophic matrixMosquito midgutPlasmodium gallinaceumTransmission-blocking interventionsBlood mealPgCHT1Mosquito midgut invasionPlasmodium ookinetesMidgut invasionParasite invasionPotential targetPeritrophic matrixMidgut epitheliumInvasionParasitesGallinaceumOokinetesMealMicroMActivity profiles