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Identification of conserved erythrocyte binding regions in members of the Plasmodium falciparum Cys6 lipid raft-associated protein family

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dc.creatorGarcía, Jeisonspa
dc.creatorCurtidor, Hernandospa
dc.creatorPinzón, Carlos G.spa
dc.creatorVanegas, Magnoliaspa
dc.creatorMoreno, Armandospa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-05-26T00:02:08Z
dc.date.available2020-05-26T00:02:08Z
dc.date.created2009spa
dc.description.abstractDetergent-resistant lipid raft membrane-associated Pf12, Pf38 and Pf41 proteins belong to the Cys6 family, whose members are implicated in Plasmodium falciparum invasion to erythrocytes. We have analyzed the interaction between 20-mer-long synthetic peptides spanning the entire Pf12, Pf38 and Pf41 sequences and erythrocytes. Eight high-activity binding peptides (HABPs) were identified in these proteins, which presented saturable bindings susceptible to erythrocytes' enzymatic treatment, and ?-turn, random coil and ?-helical elements as principal structural features. Some of these HABPs inhibited merozoite invasion in vitro, suggesting a possible role of Pf12, Pf38 and Pf41 during erythrocyte invasion and supporting their inclusion in the design of a fully effective antimalarial vaccine. © 2009 Elsevier Ltd. All rights reserved.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.vaccine.2009.04.039
dc.identifier.issn0264410X
dc.identifier.issn13588745
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23451
dc.language.isoengspa
dc.relation.citationEndPage3962
dc.relation.citationIssueNo. 30
dc.relation.citationStartPage3953
dc.relation.citationTitleVaccine
dc.relation.citationVolumeVol. 27
dc.relation.ispartofVaccine, ISSN:0264410X, 13588745, Vol.27, No.30 (2009); pp. 3953-3962spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-67349215705&doi=10.1016%2fj.vaccine.2009.04.039&partnerID=40&md5=8628b15cd242dc57a4f498392efe024aspa
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.keywordAlanylglycyllysylvalylasparaginylasparaginyllysylvalyl cysteinyllysylisoleucylglutaminylglycyllysylprolylglycylglutamyll eucylvalylglycinespa
dc.subject.keywordtertiaryeng
dc.subject.keywordAsparaginylthreonylthreonyllysylleucylasparaginylleucyl prolyllysylserylleucylasparaginylisoleucylprolylasparaginylaspartyl isoleucylleucylasparaginyltyrosinelspa
dc.subject.keywordCysteine derivativespa
dc.subject.keywordLeucylhistidyllysylasparaginyllysylvalylthreonylaspartyll eucyllysylthreonylleucylisoleucylprolylglycyltyrosylalanylseryltyrosylthreoninespa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordMembrane proteinspa
dc.subject.keywordMethionylaspartylhistidyltyrosylasparaginylasparaginyl threonylphenylalanyltyrosylserylarginylleucylprolylserylleucyl isoleucylserylaspartylasparaginyltryptophanspa
dc.subject.keywordPeptide derivativespa
dc.subject.keywordPf12 proteinspa
dc.subject.keywordPf38 proteinspa
dc.subject.keywordPf41 proteinspa
dc.subject.keywordTyrosylserylisoleucyllysylprolylaspartylglycylcysteinylphenyl alanylserylasparaginylvalyltyrosylvalyllysylarginyltyrosylprolyl asparaginylglutaminespa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordValylisoleucylglycylserylserylmethionylphenylalanylmethionyl arginylarginylserylleucylthreonylprolylasparaginyllysylisoleucyl asparaginylglutamylvalinespa
dc.subject.keywordValylleucylarginylisoleucylhistidylisoleucylserylasparaginyl glycylvalylleucylarginyllysylisoleucylprolylglycylcysteinyl aspartylphenylalanylasparaginespa
dc.subject.keywordAlpha helixspa
dc.subject.keywordArticlespa
dc.subject.keywordBeta turnspa
dc.subject.keywordBinding affinityspa
dc.subject.keywordBinding sitespa
dc.subject.keywordErythrocytespa
dc.subject.keywordHost parasite interactionspa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordLipid raftspa
dc.subject.keywordMalariaspa
dc.subject.keywordMerozoitespa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein analysisspa
dc.subject.keywordProtein functionspa
dc.subject.keywordAnimalsspa
dc.subject.keywordAntigenseng
dc.subject.keywordErythrocytesspa
dc.subject.keywordHumansspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein interaction mappingspa
dc.subject.keywordProtein structureeng
dc.subject.keywordProtein structureeng
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordReceptorseng
dc.subject.keywordAntimalarial vaccinespa
dc.subject.keywordCys6 familyspa
dc.subject.keywordHigh-activity binding peptidesspa
dc.subject.keywordPf12spa
dc.subject.keywordPf38spa
dc.subject.keywordPf41spa
dc.subject.keywordPlasmodium falciparumspa
dc.titleIdentification of conserved erythrocyte binding regions in members of the Plasmodium falciparum Cys6 lipid raft-associated protein familyspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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