2021
A 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
2001
Disruption of Plasmodium falciparumChitinase Markedly Impairs Parasite Invasion of Mosquito Midgut
Tsai Y, Hayward R, Langer R, Fidock D, Vinetz J. Disruption of Plasmodium falciparumChitinase Markedly Impairs Parasite Invasion of Mosquito Midgut. Infection And Immunity 2001, 69: 4048-4054. PMID: 11349075, PMCID: PMC98468, DOI: 10.1128/iai.69.6.4048-4054.2001.Peer-Reviewed Original ResearchConceptsMosquito midgutChitinase geneAvian malaria parasite Plasmodium gallinaceumMalaria parasite Plasmodium gallinaceumMutant ookinetesGenome databasePeritrophic matrixGene productsIntracellular traffickingBp upstreamOokinete invasionStop codonParasite invasionChitinolytic activityPfCHT1MidgutOokinetesOokinete formationGenesConfocal microscopyBlood mealApical endPlasmodium gallinaceumP. falciparumInvasion
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