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
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