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Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells

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dc.creatorArevalo-Pinzon, Gabrielaspa
dc.creatorCurtidor, Hernandospa
dc.creatorReyes, Claudiaspa
dc.creatorPinto, Marthaspa
dc.creatorVizcaíno, Carolinaspa
dc.creatorPatarroyo, Manuel A.spa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-05-25T23:56:21Z
dc.date.available2020-05-25T23:56:21Z
dc.date.created2010spa
dc.description.abstractThe Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 (1MAKLSKQQKKQMYIEKLSSL 20), HABP 33900 (41ASVRKSLRGKATILMGKNTRY60), HABP 33901 (61IRTALKKNLQAVPQIEKLLPY 80), and HABP 33906 (161LIKQGEKVTASSATLLRKFNY180). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of ?-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91%. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria. © 2009 Springer-Verlag.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1007/s00109-009-0533-5
dc.identifier.issn09462716
dc.identifier.issn14321440
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22404
dc.language.isoengspa
dc.relation.citationEndPage74
dc.relation.citationIssueNo. 1
dc.relation.citationStartPage61
dc.relation.citationTitleJournal of Molecular Medicine
dc.relation.citationVolumeVol. 88
dc.relation.ispartofJournal of Molecular Medicine, ISSN:09462716, 14321440, Vol.88, No.1 (2010); pp. 61-74spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-75749089592&doi=10.1007%2fs00109-009-0533-5&partnerID=40&md5=e9a1096adf0d5564ac641165d006348espa
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.keywordPhosphoproteinspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordErythrocytespa
dc.subject.keywordMerozoitespa
dc.subject.keywordNonhumanspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein determinationspa
dc.subject.keywordProtein synthesisspa
dc.subject.keywordRibosomespa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordErythrocytesspa
dc.subject.keywordHumansspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordRibosomal proteinsspa
dc.subject.keywordHigh activity binding peptide (habp)spa
dc.subject.keywordMalariaspa
dc.subject.keywordPeptidesspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordRed blood cells (rbcs)spa
dc.subject.keywordRibosomal phosphoprotein p0spa
dc.subject.keywordVaccinespa
dc.titleFine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cellsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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