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Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion

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dc.creatorObando-Martinez A.Z.spa
dc.creatorCurtidor H.spa
dc.creatorArévalo-Pinzón G.spa
dc.creatorVanegas M.spa
dc.creatorVizcaino C.spa
dc.creatorPatarroyo M.A.spa
dc.creatorPatarroyo M.E.spa
dc.date.accessioned2020-05-25T23:56:20Z
dc.date.available2020-05-25T23:56:20Z
dc.date.created2010spa
dc.description.abstractDetergent resistant membranes (DRMs) of Plasmodium falciparum merozoites contain a large number of glycosylphosphatidylinositol (GPI)-anchored proteins that have been implicated in interactions between merozoites and red blood cells (RBCs). In this study, two cysteine-rich proteins anchored by GPI to merozoite DRMs (Pf92 and Pf113) were studied with the aim of identifying regions actively involved in RBC invasion. By means of binding assays, high-activity binding peptides (HABPs) with a large number of binding sites per RBC were identified in Pf92 and Pf113. The nature of the RBC surface receptors for these HABPs was explored using enzyme-treated RBCs and cross-linking assays. Invasion inhibition and immunofluorescence localization studies suggest that Pf92 and Pf113 are involved in RBC invasion and that their adhesion to RBCs is mediated by such HABPs. Additionally, polymorphism and circular dichroism studies support their inclusion in further studies to design components of an antimalarial vaccine. © 2010 American Chemical Society.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1021/jm901474p
dc.identifier.issn00222623
dc.identifier.issn15204804
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22401
dc.language.isoengspa
dc.relation.citationEndPage3918
dc.relation.citationIssueNo. 10
dc.relation.citationStartPage3907
dc.relation.citationTitleJournal of Medicinal Chemistry
dc.relation.citationVolumeVol. 53
dc.relation.ispartofJournal of Medicinal Chemistry, ISSN:00222623, 15204804, Vol.53, No.10 (2010); pp. 3907-3918spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77952739304&doi=10.1021%2fjm901474p&partnerID=40&md5=f25489be2eb7f9961f8752fcac0dc128spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosariospa
dc.source.reponamereponame:Repositorio Institucional EdocURspa
dc.subject.keywordBinding proteinspa
dc.subject.keywordgeneticeng
dc.subject.keywordCysteinespa
dc.subject.keywordDetergentspa
dc.subject.keywordGlycosylphosphatidylinositolspa
dc.subject.keywordHigh activity binding peptidespa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordPf113 proteinspa
dc.subject.keywordPf92 proteinspa
dc.subject.keywordProtozoal proteinspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimal experimentspa
dc.subject.keywordAnimal modelspa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordBinding assayspa
dc.subject.keywordBinding sitespa
dc.subject.keywordCell adhesionspa
dc.subject.keywordCell invasionspa
dc.subject.keywordCircular dichroismspa
dc.subject.keywordControlled studyspa
dc.subject.keywordCross linkingspa
dc.subject.keywordErythrocytespa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordImmunofluorescencespa
dc.subject.keywordLipid raftspa
dc.subject.keywordMerozoitespa
dc.subject.keywordNonhumanspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein localizationspa
dc.subject.keywordProtein polymorphismspa
dc.subject.keywordAnimalsspa
dc.subject.keywordBinding sitesspa
dc.subject.keywordChymotrypsinspa
dc.subject.keywordCircular dichroismspa
dc.subject.keywordCross-linking reagentsspa
dc.subject.keywordCysteinespa
dc.subject.keywordDetergentsspa
dc.subject.keywordErythrocytesspa
dc.subject.keywordGlycosylphosphatidylinositolsspa
dc.subject.keywordHost-parasite interactionsspa
dc.subject.keywordImmune seraspa
dc.subject.keywordMembrane proteinsspa
dc.subject.keywordMerozoitesspa
dc.subject.keywordModelseng
dc.subject.keywordNeuraminidasespa
dc.subject.keywordPeptidesspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPolymorphismeng
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein structureeng
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordRabbitsspa
dc.subject.keywordSuccinimidesspa
dc.subject.keywordTrypsinspa
dc.titleConserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasionspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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