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A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity

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dc.creatorArévalo-Pinzón, Gabrielaspa
dc.creatorCurtidor, Hernandospa
dc.creatorMuñoz, Marinaspa
dc.creatorPatarroyo, Manuel A.spa
dc.creatorBermudez, Adrianaspa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-05-26T00:02:13Z
dc.date.available2020-05-26T00:02:13Z
dc.date.created2012spa
dc.description.abstractIdentifying the ligands or regions derived from them which parasites use to invade their target cells has proved to be an excellent strategy for identifying targets for vaccine development. Members of the reticulocyte-binding homologue family (P. fRH), including RH5, have been implicated in invasion as adhesins binding to specific receptors on erythrocyte surface. The regions mediating P. fRH5-RBC specific interactions have been identified here by fine mapping the whole P. fRH5 protein sequence. These regions, called high activity binding peptides (HABPs), bind to a receptor which is sensitive to trypsin treatment and inhibit merozoite invasion of RBCs by up to 80%, as has been found for HABP 36727. Our results show that a single amino acid change in the HABP 36727 sequence modifies a peptide's 3D structure, thereby resulting in a loss of specific binding to human RBCs and its inhibition ability, while binding to Aotus RBC remains unmodified. Such invasion differences and binding ability produced by replacing a single amino acid in an essential molecule, such as P. fRH5, highlight the inherent difficulties associated with developing a fully effective vaccine against malaria. © 2011 Elsevier Ltd.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.vaccine.2011.11.012
dc.identifier.issn0264410X
dc.identifier.issn13588745
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23459
dc.language.isoengspa
dc.relation.citationEndPage646
dc.relation.citationIssueNo. 3
dc.relation.citationStartPage637
dc.relation.citationTitleVaccine
dc.relation.citationVolumeVol. 30
dc.relation.ispartofVaccine, ISSN:0264410X, 13588745, Vol.30, No.3 (2012); pp. 637-646spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84355165243&doi=10.1016%2fj.vaccine.2011.11.012&partnerID=40&md5=6f971355b7b0c5794fe30e9bcdfaa8cfspa
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.keywordBinding proteinspa
dc.subject.keywordChloroquinespa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordMembrane proteinspa
dc.subject.keywordPlasmodium falciparum rh5 proteinspa
dc.subject.keywordTrypsinspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAmino acid analysisspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordBinding competitionspa
dc.subject.keywordBlood samplingspa
dc.subject.keywordCompetitive inhibitionspa
dc.subject.keywordControlled studyspa
dc.subject.keywordErythrocytespa
dc.subject.keywordFemalespa
dc.subject.keywordHela cellspa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordImmunogenicityspa
dc.subject.keywordParasitemiaspa
dc.subject.keywordPeptide mappingspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPolyacrylamide gel electrophoresisspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein modificationspa
dc.subject.keywordProtein structurespa
dc.subject.keywordProtein synthesisspa
dc.subject.keywordReversed phase high performance liquid chromatographyspa
dc.subject.keywordSequence analysisspa
dc.subject.keywordStructure activity relationspa
dc.subject.keywordStructure analysisspa
dc.subject.keywordWestern blottingspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAmino acid substitutionspa
dc.subject.keywordAnimalsspa
dc.subject.keywordAotus trivirgatusspa
dc.subject.keywordCarrier proteinsspa
dc.subject.keywordCell adhesionspa
dc.subject.keywordErythrocytesspa
dc.subject.keywordHumansspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordMutant proteinsspa
dc.subject.keywordMutationeng
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein conformationspa
dc.subject.keywordSequence alignmentspa
dc.subject.keywordMalariaspa
dc.subject.keywordPeptidespa
dc.subject.keywordReceptorspa
dc.subject.keywordRed blood cellspa
dc.subject.keywordStructure-activity relationshipspa
dc.subject.keywordVaccinespa
dc.titleA single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activityspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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