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Characterization of Plasmodium falciparum integral membrane protein Pf25-IMP and identification of its red blood cell binding sequences inhibiting merozoite invasion in vitro

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dc.creatorCurtidor, Hernando
dc.creatorArévalo, Gabrielaspa
dc.creatorVanegas, Magnoliaspa
dc.creatorVizcaíno, Carolinaspa
dc.creatorPatarroyo, Manuel A.spa
dc.creatorForero, Marthaspa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-05-25T23:58:36Z
dc.date.available2020-05-25T23:58:36Z
dc.date.created2008spa
dc.description.abstractThe identification of proteins present on the surface of Plasmodium falciparum-infected red blood cells as well as of free merozoites has been widely considered as one of the main areas of research in the development of an antimalarial vaccine due to their involvement in the parasite's pathogenesis and invasion mechanisms. Major advances had been accomplished in this area thanks to the analysis of the reported genomic sequence of P. falciparum, allowing for the identification of genes encoding for putative integral membrane proteins. This study reports for the first time the transcription of the MAL8P1.3 gene, which codifies for a 25-kDa integral membrane protein of P. falciparum (FCB-2 strain), namely, Pf25-IMP. Western blot and immunofluorescence assays using goat polyclonal sera indicate that this protein is expressed in erythrocytic asexual blood stages. A highly robust, sensible, and specific receptor-ligand interaction assay allowed identification of two high activity binding peptides (HABPs) derived from Pf25-IMP: 30577 (41YKTANENVKLASSLSDRLSR 60) and 30583 (161LNKKTVVRKIAEGLGYTIVF180). Both HABPs bound with high affinity to human red blood cells (RBCs), and such binding was susceptible to enzyme treatment with trypsin. A common RBC surface receptor of apparently 48 kDa was found for both HABPs, plus an additional 31-kDa receptor for HABP 30577. HABP 30577 inhibited merozoite invasion in vitro by 73%, while HABP 30583 showed a 59% inhibition at 200 ?M concentration. The data suggest a possible role of Pf25-IMP in merozoite invasion to RBCs and support its inclusion in further immunological studies for evaluating its potential as vaccine candidates. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1110/ps.036251.108
dc.identifier.issn9618368
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22894
dc.language.isoengspa
dc.relation.citationEndPage1504
dc.relation.citationIssueNo. 9
dc.relation.citationStartPage1494
dc.relation.citationTitleProtein Science
dc.relation.citationVolumeVol. 17
dc.relation.ispartofProtein Science, ISSN:9618368, Vol.17, No.9 (2008); pp. 1494-1504spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-50049135211&doi=10.1110%2fps.036251.108&partnerID=40&md5=7e6abd3c693a90e0dcd69a2009f04c66spa
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.keywordAmino acidspa
dc.subject.keywordsecondaryeng
dc.subject.keywordMembrane proteinspa
dc.subject.keywordPf25 membrane proteinspa
dc.subject.keywordTyrosyllysylthreonylalanylasparaginylglutamylasparaginylvalyllysyl leucylalanylserylserylleucylserylaspartylarginylleucylserylargininespa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordControlled studyspa
dc.subject.keywordErythrocytespa
dc.subject.keywordGenespa
dc.subject.keywordGenetic transcriptionspa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordImmunofluorescencespa
dc.subject.keywordMal8p1.3 genespa
dc.subject.keywordMerozoitespa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein analysisspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordWestern blottingspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordBase sequencespa
dc.subject.keywordBinding sitesspa
dc.subject.keywordCellseng
dc.subject.keywordChymotrypsinspa
dc.subject.keywordDose-response relationshipeng
dc.subject.keywordErythrocytesspa
dc.subject.keywordGeneseng
dc.subject.keywordHumansspa
dc.subject.keywordMembrane proteinsspa
dc.subject.keywordMerozoitesspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordMolecular weightspa
dc.subject.keywordNeuraminidasespa
dc.subject.keywordPeptide fragmentsspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein structureeng
dc.subject.keywordProtein structureeng
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordSequence homologyeng
dc.subject.keywordTranscriptioneng
dc.subject.keywordTrypsinspa
dc.subject.keywordCapra hircusspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordBinding assayspa
dc.subject.keywordPf25-impspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordRed blood cellspa
dc.subject.keywordSynthetic peptidespa
dc.titleCharacterization of Plasmodium falciparum integral membrane protein Pf25-IMP and identification of its red blood cell binding sequences inhibiting merozoite invasion in vitrospa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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