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Well-defined regions of the Plasmodium falciparum reticulocyte binding protein homologue 4 mediate interaction with red blood cell membrane

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dc.creatorGarcía J.spa
dc.creatorCurtidor H.spa
dc.creatorPinzón C.G.spa
dc.creatorPatarroyo M.A.spa
dc.creatorVanegas M.spa
dc.creatorForero M.spa
dc.creatorPatarroyo M.E.spa
dc.date.accessioned2020-05-25T23:56:21Z
dc.date.available2020-05-25T23:56:21Z
dc.date.created2010spa
dc.description.abstractTwo widely studied parasite protein families are considered attractive targets for developing a fully effective antimalarial vaccine: the erythrocyte binding antigen (EBA) family defining a sialic acid-dependent invasion pathway, and reticulocyte-binding homologue (RH) proteins associated with sialic acid-independent red blood cell (RBC) invasion. In this study, the micronemal invasive PfRH4 protein was finely mapped using 20-mer-long synthetic peptides spanning the entire protein length to identify protein regions that establish high affinity interactions with human RBCs. Twenty conserved, mainly ?-helical high-activity binding peptides (HABPs) with nanomolar dissociation constants and recognizing 32, 25, 22, and 20 kDaRBCmembrane molecules in a chymotrypsin and/or trypsin-sensitive manner were identified in this protein. Anti-PfRH4 rabbit sera and PfRH4 HABPs inhibited merozoite invasion in vitro, therefore suggesting the implication of these HABPs in Plasmodium falciparum invasion and supporting their inclusion in further structural and immunological studies to design potential components of a minimal subunit-based, multiantigenic, chemically synthesized antimalarial vaccine. ©2009 American Chemical Society.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1021/jm901540n
dc.identifier.issn00222623
dc.identifier.issn15204804
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22402
dc.language.isoengspa
dc.relation.citationEndPage821
dc.relation.citationIssueNo. 2
dc.relation.citationStartPage811
dc.relation.citationTitleJournal of Medicinal Chemistry
dc.relation.citationVolumeVol. 53
dc.relation.ispartofJournal of Medicinal Chemistry, ISSN:00222623, 15204804, Vol.53, No.2 (2010); pp. 811-821spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77249163223&doi=10.1021%2fjm901540n&partnerID=40&md5=82161b04987854a392acf66842dde100spa
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 surface receptorspa
dc.subject.keywordReticulocyte binding protein homolog 4spa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordCell invasionspa
dc.subject.keywordControlled studyspa
dc.subject.keywordDissociation constantspa
dc.subject.keywordErythrocyte membranespa
dc.subject.keywordHumanspa
dc.subject.keywordHuman tissuespa
dc.subject.keywordMalariaspa
dc.subject.keywordMembrane bindingspa
dc.subject.keywordNormal humanspa
dc.subject.keywordNucleotide sequencespa
dc.subject.keywordPeptide mappingspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordAnimalsspa
dc.subject.keywordBinding sitesspa
dc.subject.keywordErythrocyte membranespa
dc.subject.keywordMembrane proteinsspa
dc.subject.keywordPeptide fragmentsspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein interaction mappingspa
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordRabbitsspa
dc.titleWell-defined regions of the Plasmodium falciparum reticulocyte binding protein homologue 4 mediate interaction with red blood cell membranespa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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