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 mechanismProteinChitinasesMidgutChitinase
2001
Plasmodium 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 ResearchMeSH KeywordsAnimalsAnimals, Genetically ModifiedChitinasesCulicidaeHost-Parasite InteractionsModels, MolecularPlasmodiumConceptsMosquito midgutMalaria transmission-blocking strategiesParasite-mosquito interactionsTransmission-blocking strategiesTransmission-blocking drugsGlobal malaria controlPeritrophic matrixMalaria transmissionTransgenic mosquitoesMalaria controlCandidate targetsChitinasesMidgutChitinaseCrucial roleVaccine
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