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
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 Research
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