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Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes

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dc.creatorPinzón, Carlos Giovannispa
dc.creatorCurtidor, Hernandospa
dc.creatorGarcía, Jeisonspa
dc.creatorVanegas, Magnoliaspa
dc.creatorVizcaíno, Carolinaspa
dc.creatorPatarroyo, Manuel A.spa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-05-26T00:02:10Z
dc.date.available2020-05-26T00:02:10Z
dc.date.created2010spa
dc.description.abstractIn this study, we synthesized the complete sequence of the CLAG-9 protein as 67 20-mer-long non-overlapped peptides and assessed their ability to bind to erythrocytes in receptor-ligand assays. Twenty CLAG-9 peptides were found to have specific high-affinity binding ability to erythrocytes (thereby named as HABPs), with nanomolar dissociation constants. CLAG-9 HABPs interacted with different erythrocyte surface receptors having apparent molecular weights of 85, 63 and 34 kDa. CLAG-9 HABPs binding was also affected by pre-treatment of RBCs with enzymes and inhibited erythrocyte invasion in vitro by up to 72% at 200 ?M. These results suggest that some protein fragments of CLAG-9 may be part of the molecular machinery used by malaria parasites to invade erythrocytes, hence supporting their study as possible vaccine candidates. © 2010 Elsevier Ltd. All rights reserved.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.vaccine.2010.01.004
dc.identifier.issn0264410X
dc.identifier.issn13588745
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23454
dc.language.isoengspa
dc.relation.citationEndPage2663
dc.relation.citationIssueNo. 14
dc.relation.citationStartPage2653
dc.relation.citationTitleVaccine
dc.relation.citationVolumeVol. 28
dc.relation.ispartofVaccine, ISSN:0264410X, 13588745, Vol.28, No.14 (2010); pp. 2653-2663spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77649180960&doi=10.1016%2fj.vaccine.2010.01.004&partnerID=40&md5=05707e9cf97d0ed0d5e8161e25678244spa
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.keywordCell receptorspa
dc.subject.keywordfalciparumeng
dc.subject.keywordProtozoal proteinspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordCell invasionspa
dc.subject.keywordDissociation constantspa
dc.subject.keywordErythrocytespa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordMolecular weightspa
dc.subject.keywordNonhumanspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein interactionspa
dc.subject.keywordProtein synthesisspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordCell adhesion moleculesspa
dc.subject.keywordErythrocytesspa
dc.subject.keywordHumansspa
dc.subject.keywordKineticsspa
dc.subject.keywordMalariaeng
dc.subject.keywordMembrane proteinsspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordMolecular weightspa
dc.subject.keywordPeptide hydrolasesspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordVirulence factorsspa
dc.subject.keywordAntimalarial vaccinespa
dc.subject.keywordCytoadherence-linked asexual protein 9spa
dc.subject.keywordPlasmodium falciparumspa
dc.titleSequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytesspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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