2022
Structure–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 ResearchConceptsPutative 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
2021
Evolutionary Insights into the Microneme-Secreted, Chitinase-Containing High-Molecular-Weight Protein Complexes Involved in Plasmodium Invasion of the Mosquito Midgut
Kaur H, Pacheco MA, Garber L, Escalante AA, Vinetz JM. Evolutionary Insights into the Microneme-Secreted, Chitinase-Containing High-Molecular-Weight Protein Complexes Involved in Plasmodium Invasion of the Mosquito Midgut. Infection And Immunity 2021, 90: e00314-21. PMID: 34606368, PMCID: PMC8788677, DOI: 10.1128/iai.00314-21.Peer-Reviewed Original ResearchConceptsPeritrophic matrixMosquito midgutNew genomic insightsWeight protein complexesHigh-resolution structural modelingDomain-related proteinEvolutionary insightsInvasion machineryGenomic insightsMicronemal proteinsProtein complexesThree-dimensional structureMosquito interactionsGenomic dataPlasmodium invasionProteolytic milieuMidgut epitheliumWeight complexesAdhesive proteinsOokinetesGeneral mechanismProteinChitinasesMidgutChitinaseA Hetero-Multimeric Chitinase-Containing Plasmodium falciparum and Plasmodium gallinaceum Ookinete-Secreted Protein Complex Involved in Mosquito Midgut Invasion
Patra KP, Kaur H, Kolli SK, Wozniak JM, Prieto JH, Yates JR, Gonzalez DJ, Janse CJ, Vinetz JM. A Hetero-Multimeric Chitinase-Containing Plasmodium falciparum and Plasmodium gallinaceum Ookinete-Secreted Protein Complex Involved in Mosquito Midgut Invasion. Frontiers In Cellular And Infection Microbiology 2021, 10: 615343. PMID: 33489941, PMCID: PMC7821095, DOI: 10.3389/fcimb.2020.615343.Peer-Reviewed Original ResearchConceptsChitin-containing peritrophic matrixHMW complexesMosquito midgut invasionDomain-related proteinNext-generation vaccinesMicronemal proteinsVon Willebrand factorProtein complexesMidgut invasionPeritrophic matrixProteolytic milieuMidgut epitheliumPfCHT1Malaria parasitesSurface enolaseOokinetesPlasmodium falciparumWillebrand factorMidgut wallAdhesive proteinsProteinMass spectrometryShort formSize exclusion chromatography dataMosquito vectors
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 ResearchKnockout 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 transmissionPlasmodium ookinete-secreted chitinase and parasite penetration of the mosquito peritrophic matrix
Langer R, Vinetz J. Plasmodium ookinete-secreted chitinase and parasite penetration of the mosquito peritrophic matrix. Trends In Parasitology 2001, 17: 269-272. PMID: 11378031, DOI: 10.1016/s1471-4922(01)01918-3.Peer-Reviewed Original ResearchConceptsMosquito midgutMalaria transmission-blocking strategiesParasite-mosquito interactionsTransmission-blocking strategiesTransmission-blocking drugsGlobal malaria controlPeritrophic matrixMalaria transmissionTransgenic mosquitoesMalaria controlCandidate targetsChitinasesMidgutChitinaseCrucial roleVaccine
2000
Micronemal Transport of Plasmodium Ookinete Chitinases to the Electron-Dense Area of the Apical Complex for Extracellular Secretion
Langer R, Hayward R, Tsuboi T, Tachibana M, Torii M, Vinetz J. Micronemal Transport of Plasmodium Ookinete Chitinases to the Electron-Dense Area of the Apical Complex for Extracellular Secretion. Infection And Immunity 2000, 68: 6461-6465. PMID: 11035760, PMCID: PMC97734, DOI: 10.1128/iai.68.11.6461-6465.2000.Peer-Reviewed Original ResearchChitinases 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 oligomersChitinases of human parasites and their implications as antiparasitic targets.
Shahabuddin M, Vinetz J. Chitinases of human parasites and their implications as antiparasitic targets. EXS 1999, 87: 223-34. PMID: 10906963, DOI: 10.1007/978-3-0348-8757-1_16.Peer-Reviewed Original ResearchConceptsDevelopmental stage-specific mannerStage-specific mannerAmino acid sequenceChitin-containing structuresPathogenic parasitesAnimal diseasesAntiparasitic targetsChitinase geneInsect vectorsAcid sequenceSuccessful infectionChitinasesHuman parasitesParasitesNumber of humanGenesLife cycleChitinAnimal bodyPathogensRecent studiesHarsh conditionsVertebratesChitinaseOrganisms
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