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
Knockout of the Rodent Malaria Parasite Chitinase PbCHT1 Reduces Infectivity to Mosquitoes
Dessens J, Mendoza J, Claudianos C, Vinetz J, Khater E, Hassard S, Ranawaka G, Sinden R. Knockout of the Rodent Malaria Parasite Chitinase PbCHT1 Reduces Infectivity to Mosquitoes. Infection And Immunity 2001, 69: 4041-4047. PMID: 11349074, PMCID: PMC98467, DOI: 10.1128/iai.69.6.4041-4047.2001.Peer-Reviewed Original ResearchConceptsPeritrophic matrixChitinase geneChitinase activityHuman malaria parasite Plasmodium falciparumMalaria parasite Plasmodium falciparumPlasmodium-mosquito interactionsAvian malaria parasite Plasmodium gallinaceumAvian malaria transmissionParasite Plasmodium falciparumMalaria parasite Plasmodium gallinaceumChitin-containing structuresNull mutantsRodent malaria parasiteInfected blood mealMalaria ookinetesTransmission-blocking drugsAnopheles stephensi mosquitoesMidgut invasionStructural orthologsMosquito midgutOokinete invasionPM disruptionMidgut epitheliumTargeted disruptionMalaria transmission
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
1999
The chitinase PfCHT1 from the human malaria parasite Plasmodium falciparum lacks proenzyme and chitin-binding domains and displays unique substrate preferences
Vinetz J, Dave S, Specht C, Brameld K, Xu B, Hayward R, Fidock D. The chitinase PfCHT1 from the human malaria parasite Plasmodium falciparum lacks proenzyme and chitin-binding domains and displays unique substrate preferences. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 14061-14066. PMID: 10570198, PMCID: PMC24190, DOI: 10.1073/pnas.96.24.14061.Peer-Reviewed Original ResearchMeSH KeywordsAcetylglucosamineAmino Acid SequenceAnimalsBase SequenceBinding SitesChitinChitinasesEnzyme ActivationEnzyme InhibitorsEnzyme PrecursorsGene ExpressionGenes, ProtozoanHumansHydrogen-Ion ConcentrationMalariaModels, MolecularMolecular Sequence DataPlasmodium falciparumProtein ConformationProtozoan ProteinsSequence Homology, Amino AcidSubstrate SpecificityTrisaccharidesConceptsP. gallinaceumHuman malaria transmissionMosquito midgut epitheliumChitinase geneHuman malaria parasite Plasmodium falciparumChitin-binding domainMalaria parasite Plasmodium falciparumPfCHT1PgCHT1Malaria transmissionParasite Plasmodium falciparumPeritrophic matrixSubstrate preferenceP. falciparum genome databasePlasmodium falciparumMosquito midgutOocyst developmentParasite invasionBlood mealActive recombinant enzymeP. falciparum genesUnique substrate preferenceDifferential sensitivityGenome databaseHexameric oligomers
1998
Plasmodium gallinaceum: Use of Antisera to Degenerate Synthetic Peptides Derived from the Active Site of Protozoal Chitinases to Characterize an Ookinete-Specific Chitinase
Vinetz J, Kaslow D. Plasmodium gallinaceum: Use of Antisera to Degenerate Synthetic Peptides Derived from the Active Site of Protozoal Chitinases to Characterize an Ookinete-Specific Chitinase. Experimental Parasitology 1998, 90: 199-202. PMID: 9769251, DOI: 10.1006/expr.1998.4322.Peer-Reviewed Original Research