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Binding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteins

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dc.creatorCurtidor, Hernando
dc.creatorArévalo-Pinzón, Gabrielaspa
dc.creatorBermudez, Adrianaspa
dc.creatorCalderon, Dayanaspa
dc.creatorVanegas, Magnoliaspa
dc.creatorPatiño, Liliana C.spa
dc.creatorPatarroyo, Manuel A.spa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-05-26T00:10:51Z
dc.date.available2020-05-26T00:10:51Z
dc.date.created2012spa
dc.description.abstractSeveral sporozoite proteins have been associated with Plasmodium falciparum cell traversal and hepatocyte invasion, including the cell-traversal protein for ookinetes and sporozoites (CelTOS), and thrombospondin-related sporozoite protein (TRSP). CelTOS and TRSP amino acid sequences have been finely mapped to identify regions specifically binding to HeLa and HepG2 cells, respectively. Three high-activity binding peptides (HABPs) were found in CelTOS and one HABP was found in TRSP, all of them having high ?-helical structure content. These HABPs' specific binding was sensitive to HeLa and HepG2 cells' pre-treatment with heparinase I and chondroitinase ABC. Despite their similarity at three-dimensional (3D) structural level, TRSP and TRAP HABPs located in the TSR domain did not compete for the same binding sites. CelTOS and TRSP HABPs were used as a template for designing modified sequences to then be assessed in the Aotus monkey experimental model. Antibodies directed against these modified HABPs were able to recognize both the native parasite protein by immunofluorescence assay and the recombinant protein (expressed in Escherichia coli) by Western blot and ELISA assays. The results suggested that these modified HABPs could be promising targets in designing a fully effective, antimalarial vaccine. © 2011 Springer-Verlag.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1007/s00726-011-1087-8
dc.identifier.issn09394451
dc.identifier.issn14382199
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/24263
dc.language.isoengspa
dc.relation.citationEndPage378
dc.relation.citationIssueNo. 1
dc.relation.citationStartPage365
dc.relation.citationTitleAmino Acids
dc.relation.citationVolumeVol. 43
dc.relation.ispartofAmino Acids, ISSN:09394451, 14382199, Vol.43, No.1 (2012); pp. 365-378spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84862754189&doi=10.1007%2fs00726-011-1087-8&partnerID=40&md5=9d0735a2cbe9348df324fbdcd7ab9947spa
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.keywordCell traversal proteinspa
dc.subject.keywordsecondaryeng
dc.subject.keywordHeparin lyasespa
dc.subject.keywordHigh activity binding peptidespa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordProtozoal proteinspa
dc.subject.keywordSynthetic peptidespa
dc.subject.keywordThrombospondin related sporozoite proteinspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAlpha helixspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimal experimentspa
dc.subject.keywordArticlespa
dc.subject.keywordBinding sitespa
dc.subject.keywordCell strain hepg2spa
dc.subject.keywordControlled studyspa
dc.subject.keywordDrug targetingspa
dc.subject.keywordEnzyme linked immunosorbent assayspa
dc.subject.keywordHaplorhinispa
dc.subject.keywordHela cellspa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordImmunogenicityspa
dc.subject.keywordMalaria falciparumspa
dc.subject.keywordNonhumanspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein domainspa
dc.subject.keywordProtein structurespa
dc.subject.keywordWestern blottingspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordAotus trivirgatusspa
dc.subject.keywordBinding sitesspa
dc.subject.keywordCell lineeng
dc.subject.keywordChondroitin abc lyasespa
dc.subject.keywordHela cellsspa
dc.subject.keywordHep g2 cellsspa
dc.subject.keywordHeparin lyasespa
dc.subject.keywordHepatocytesspa
dc.subject.keywordHumansspa
dc.subject.keywordMalaria vaccinesspa
dc.subject.keywordPeptidesspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein structureeng
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordRecombinant proteinsspa
dc.subject.keywordSporozoitesspa
dc.subject.keywordThrombospondinsspa
dc.subject.keywordEscherichia colispa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordCeltosspa
dc.subject.keywordPeptidespa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordSporozoitespa
dc.subject.keywordTrspspa
dc.subject.keywordVaccinespa
dc.titleBinding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteinsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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