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dc.creatorArevalo-Pinzon, Gabriela 
dc.creatorCurtidor, Hernando 
dc.creatorReyes, Claudia 
dc.creatorPinto, Martha 
dc.creatorVizcaíno, Carolina 
dc.creatorPatarroyo, Manuel A. 
dc.creatorPatarroyo, Manuel E. 
dc.date.accessioned2020-05-25T23:56:21Z
dc.date.available2020-05-25T23:56:21Z
dc.date.created2010
dc.identifier.issn09462716
dc.identifier.issn14321440
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22404
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.
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.relation.ispartofJournal of Molecular Medicine, ISSN:09462716, 14321440, Vol.88, No.1 (2010); pp. 61-74
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-75749089592&doi=10.1007%2fs00109-009-0533-5&partnerID=40&md5=e9a1096adf0d5564ac641165d006348e
dc.titleFine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells
dc.typearticle
dc.subject.keywordPhosphoprotein
dc.subject.keywordAmino acid sequence
dc.subject.keywordArticle
dc.subject.keywordErythrocyte
dc.subject.keywordMerozoite
dc.subject.keywordNonhuman
dc.subject.keywordPlasmodium falciparum
dc.subject.keywordProtein binding
dc.subject.keywordProtein determination
dc.subject.keywordProtein synthesis
dc.subject.keywordRibosome
dc.subject.keywordAmino acid sequence
dc.subject.keywordErythrocytes
dc.subject.keywordHumans
dc.subject.keywordMolecular sequence data
dc.subject.keywordPlasmodium falciparum
dc.subject.keywordProtein binding
dc.subject.keywordProtozoan proteins
dc.subject.keywordRibosomal proteins
dc.subject.keywordHigh activity binding peptide (habp)
dc.subject.keywordMalaria
dc.subject.keywordPeptides
dc.subject.keywordPlasmodium falciparum
dc.subject.keywordRed blood cells (rbcs)
dc.subject.keywordRibosomal phosphoprotein p0
dc.subject.keywordVaccine
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.type.spaArtículo
dc.rights.accesoAbierto (Texto Completo)
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doihttps://doi.org/10.1007/s00109-009-0533-5
dc.relation.citationEndPage74
dc.relation.citationIssueNo. 1
dc.relation.citationStartPage61
dc.relation.citationTitleJournal of Molecular Medicine
dc.relation.citationVolumeVol. 88
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR


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