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Conserved regions of the Plasmodium falciparum rhoptry-associated protein 3 mediate specific host-pathogen interactions during invasion of red blood cells

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dc.creatorGarcía, Jeisonspa
dc.creatorCurtidor, Hernandospa
dc.creatorVanegas, Magnoliaspa
dc.creatorArévalo-Pinzon, Gabrielaspa
dc.creatorPatarroyo, Manuel A.spa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-05-25T23:58:01Z
dc.date.available2020-05-25T23:58:01Z
dc.date.created2010spa
dc.description.abstractInvasion of red blood cells (RBCs) by the Plasmodium falciparum malaria merozoite is mediated by parasite surface molecules and proteins contained within apical organelles that are capable of recognizing receptors on the membrane of RBCs. The identification and characterization of these P. falciparum invasion-associated proteins is the first step for unveiling potential new drug and vaccine target molecules to eradicate this deadly disease. Among the exclusive set of malarial vaccine candidates, the members of the rhoptry-associated protein (RAP) family have been associated with the parasite's binding to and invasion of RBCs. Remarkably, the third member of this family (named RAP-3) has been recently detected on the surface of non-infected RBCs exposed to free merozoites, therefore suggesting the participation of this protein during RBC infection. In this study, the sequence of RAP-3 was finely mapped using synthetic peptides in order to identify which are the specific binding regions involved in RAP3-RBC interactions. Two high-activity binding peptides (HABPs) established high affinity interactions with RBC surface molecules of about 27-90 kDa, which were differentially affected by different enzymatic treatments. RAP-1 and RAP-2 HABPs inhibited binding of RAP-3 HABPs to different extents, thus suggesting the recognition of similar binding sites on RBC membrane, as well as ability of RAP-3 HABPs to inhibit P. falciparum infection in vitro. Altogether, these functional analyses of RAP-3 HABPs strongly suggest a potential role for this protein in RBC invasion, and highlight its HABPs as potential targets to develop a fully protective minimal subunit-based malarial vaccine. © 2010 Elsevier Inc. All rights reserved.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.peptides.2010.09.002
dc.identifier.issn1969781
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22786
dc.language.isoengspa
dc.relation.citationEndPage2172
dc.relation.citationIssueNo. 12
dc.relation.citationStartPage2165
dc.relation.citationTitlePeptides
dc.relation.citationVolumeVol. 31
dc.relation.ispartofPeptides, ISSN:1969781, Vol.31, No.12 (2010); pp. 2165-2172spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-78049458485&doi=10.1016%2fj.peptides.2010.09.002&partnerID=40&md5=b569aa4ac4ab4dd28afcd4004df50cb7spa
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.keywordProtozoal proteinspa
dc.subject.keywordsecondaryeng
dc.subject.keywordRhoptry associated protein 2spa
dc.subject.keywordRhoptry associated protein 3spa
dc.subject.keywordSynthetic peptidespa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordBinding sitespa
dc.subject.keywordCell invasionspa
dc.subject.keywordCell surfacespa
dc.subject.keywordControlled studyspa
dc.subject.keywordErythrocytespa
dc.subject.keywordErythrocyte membranespa
dc.subject.keywordGene mappingspa
dc.subject.keywordHost parasite interactionspa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordIn vitro studyspa
dc.subject.keywordMolecular interactionspa
dc.subject.keywordMolecular recognitionspa
dc.subject.keywordMolecular sizespa
dc.subject.keywordNonhumanspa
dc.subject.keywordNucleotide sequencespa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein analysisspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein functionspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordBinding sitesspa
dc.subject.keywordCellseng
dc.subject.keywordErythrocytesspa
dc.subject.keywordHost-pathogen interactionsspa
dc.subject.keywordHumansspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein structureeng
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordHabpsspa
dc.subject.keywordHigh-activity binding peptidesspa
dc.subject.keywordMalarial vaccinespa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordRap-3spa
dc.subject.keywordRhoptry-associated protein 3spa
dc.titleConserved regions of the Plasmodium falciparum rhoptry-associated protein 3 mediate specific host-pathogen interactions during invasion of red blood cellsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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