2024
Genomic surveillance of malaria parasites in an indigenous community in the Peruvian Amazon
Cabrera-Sosa L, Nolasco O, Kattenberg J, Fernandez-Miñope C, Valdivia H, Barazorda K, Arévalo de los Rios S, Rodriguez-Ferrucci H, Vinetz J, Rosanas-Urgell A, Van geertruyden J, Gamboa D, Delgado-Ratto C. Genomic surveillance of malaria parasites in an indigenous community in the Peruvian Amazon. Scientific Reports 2024, 14: 16291. PMID: 39009685, PMCID: PMC11250820, DOI: 10.1038/s41598-024-66925-x.Peer-Reviewed Original ResearchConceptsPassive case detectionPf parasitesPersistent malaria transmissionPfhrp2/3 gene deletionsDeep sequencing assaySulfadoxine-pyrimethamineMalaria casesMalaria eliminationPlasmodium vivaxMalaria parasitesMalaria transmissionP. falciparumResistance mutationsImported infectionsMalariaPopulation genetic indicesSequencing assayCase detectionGene deletionPV populationResistance markersGenetic diversityPeruvian AmazonGenomic surveillanceGenetic indices
2022
Geographical distribution and genetic characterization of pfhrp2 negative Plasmodium falciparum parasites in the Peruvian Amazon
Bendezu J, Torres K, Villasis E, Incardona S, Bell D, Vinetz J, Gamboa D. Geographical distribution and genetic characterization of pfhrp2 negative Plasmodium falciparum parasites in the Peruvian Amazon. PLOS ONE 2022, 17: e0273872. PMID: 36413547, PMCID: PMC9681099, DOI: 10.1371/journal.pone.0273872.Peer-Reviewed Original ResearchStructure–function analysis of cysteine residues in the plasmodium falciparum chitinase, PfCHT1
Kaur H, Garber L, Murphy JW, Vinetz JM. Structure–function analysis of cysteine residues in the plasmodium falciparum chitinase, PfCHT1. Protein Science 2022, 31: e4289. PMID: 35481637, PMCID: PMC8994504, DOI: 10.1002/pro.4289.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArtificial IntelligenceChitinChitinasesCysteineDisulfidesEscherichia coliHumansMosquito VectorsPlasmodium falciparumProtozoan ProteinsConceptsPutative chitin-binding domainChitin-binding domainPlasmodium ookinetesProtein-protein interactionsRecombinant protein productionIntermolecular protein-protein interactionsMosquito midgut invasionStructure-function analysisEnzymatic activityIntramolecular disulfide linkagesIntermolecular disulfide bondingChitin-containing peritrophic matrixParasite cladesMidgut invasionPeritrophic matrixCysteine residuesProtein productionChitinase activityBiochemical studiesDisulfide bondingUnpaired cysteineChitinaseMalaria parasitesE. coliMutants
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