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Conserved regions from Plasmodium falciparum MSP11 specifically interact with host cells and have a potential role during merozoite invasion of red blood cells

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dc.creatorObando?Martinez, Ana Zuleimaspa
dc.creatorCurtidor, Hernandospa
dc.creatorVanegas, Magnoliaspa
dc.creatorArévalo?Pinzón, Gabrielaspa
dc.creatorPatarroyo, Manuel A.
dc.creatorPatarroyo, Manuel Elkinspa
dc.date.accessioned2020-05-25T23:55:58Z
dc.date.available2020-05-25T23:55:58Z
dc.date.created2010spa
dc.description.abstractDespite significant global efforts, a completely effective vaccine against Plasmodium falciparum, the species responsible for the most serious form of malaria, has not been yet obtained. One of the most promising approaches consists in combining chemically synthesized minimal subunits of parasite proteins involved in host cell invasion, which has led to the identification of peptides with high binding activity (named HABPs) to hepatocyte and red blood cell (RBC) surface receptors in a large number of sporozoite and merozoite proteins, respectively. Among these proteins is the merozoite surface protein 11 (MSP11), which shares important structural and immunological features with the antimalarial vaccine candidates MSP1, MSP3, and MSP6. In this study, 20-mer-long synthetic peptides spanning the complete sequence of MSP11 were assessed for their ability to bind specifically to RBCs. Two HABPs with high ability to inhibit invasion of RBCs in vitro were identified (namely HABPs 33595 and 33606). HABP-RBC bindings were characterized by means of saturation assays and Hill analysis, finding cooperative interactions of high affinity for both HABPs (nH of 1.5 and 1.2, Kd of 800 and 600nM for HABPs 33595 and 33606, respectively). The nature of the possible RBC receptors for MSP11 HABPs was studied in binding assays to enzyme-treated RBCs and cross-linking assays, finding that both HABPs use mainly a sialic acid-dependent receptor. An analysis of the immunological, structural and polymorphic characteristics of MSP11 HABPs supports including these peptides in further studies with the aim of designing a fully effective protection-inducing vaccine against malaria. © 2010 Wiley-Liss, Inc.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1002/jcb.22600
dc.identifier.issn07302312
dc.identifier.issn10974644
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22279
dc.language.isoengspa
dc.publisherWiley-Liss Inc.spa
dc.relation.citationEndPage892
dc.relation.citationIssueNo. 4
dc.relation.citationStartPage882
dc.relation.citationTitleJournal of Cellular Biochemistry
dc.relation.citationVolumeVol. 110
dc.relation.ispartofJournal of Cellular Biochemistry, ISSN:07302312, 10974644, Vol.110, No.4 (2010); pp. 882-892spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77954117696&doi=10.1002%2fjcb.22600&partnerID=40&md5=5e4487713ac6712e51297c441910eda4spa
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.keywordMerozoite surface protein 1spa
dc.subject.keywordMerozoite surface protein 11spa
dc.subject.keywordSialic acidspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtozoal proteinspa
dc.subject.keywordArticlespa
dc.subject.keywordControlled studyspa
dc.subject.keywordCross linkingspa
dc.subject.keywordErythrocytespa
dc.subject.keywordHost parasite interactionspa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordMerozoitespa
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 structurespa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalspa
dc.subject.keywordChemistryspa
dc.subject.keywordGenetic polymorphismspa
dc.subject.keywordGeneticsspa
dc.subject.keywordMetabolismspa
dc.subject.keywordMolecular geneticsspa
dc.subject.keywordMolecular weightspa
dc.subject.keywordNucleotide sequencespa
dc.subject.keywordParasitologyspa
dc.subject.keywordPhysiologyspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein secondary structurespa
dc.subject.keywordSequence homologyspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordBase sequencespa
dc.subject.keywordConserved sequencespa
dc.subject.keywordErythrocytesspa
dc.subject.keywordMerozoitesspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordMolecular weightspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPolymorphismeng
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein structure, secondaryspa
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordSequence homologyeng
dc.subject.keywordSequence homologyeng
dc.subject.keywordAntimalarial vaccinespa
dc.subject.keywordH103spa
dc.subject.keywordMerozoite invasion of red blood cellsspa
dc.subject.keywordMerozoite surface protein 11spa
dc.subject.keywordMolecular interactions host-pathogenspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordSynthetic peptidesspa
dc.titleConserved regions from Plasmodium falciparum MSP11 specifically interact with host cells and have a potential role during merozoite invasion of red blood cellsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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