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Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein

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dc.creatorSaravia, Carolinaspa
dc.creatorMartinez, Paolaspa
dc.creatorGranados, Diana S.spa
dc.creatorLopez, Carolinaspa
dc.creatorReyes, Claudiaspa
dc.creatorPatarroyo, Manuel A.spa
dc.date.accessioned2020-05-26T00:02:35Z
dc.date.available2020-05-26T00:02:35Z
dc.date.created2008spa
dc.description.abstractSelected PvDBP-derived synthetic peptides were tested in competition assays with HLA molecules in order to identify and evaluate their binding to a wide range of MHC class II molecules. Binding was evaluated as the peptide's ability to displace the biotinylated control peptide (HA306-318) and was detected by a conventional ELISA. Thus, one epitope for the HLA-DR1 molecule, two epitopes for the HLA-DR4 molecule, six epitopes for the HLA-DR7 molecule and three epitopes for the HLA-DR11 molecule displaying a high binding percentage (above 50%) were experimentally obtained. The in vitro results were compared with the epitope prediction results. Two peptides behaved as universal epitopes since they bound to a larger number of HLA-DR molecules. Given that these peptides are located in the conserved PvDBP region II, they could be considered good candidates to be included in the design of a synthetic vaccine against Plasmodium vivax malaria. © 2008 Elsevier Inc. All rights reserved.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2008.10.153
dc.identifier.issn0006-291X
dc.identifier.issn1090-2104
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23504
dc.language.isoengspa
dc.relation.citationEndPage1283
dc.relation.citationIssueNo. 4
dc.relation.citationStartPage1279
dc.relation.citationTitleBiochemical and Biophysical Research Communications
dc.relation.citationVolumeVol. 377
dc.relation.ispartofBiochemical and Biophysical Research Communications, ISSN:0006-291X, 1090-2104, Vol.377, No.4 (2008); pp. 1279-1283spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-56349138132&doi=10.1016%2fj.bbrc.2008.10.153&partnerID=40&md5=43e85aaec428ebeae8cf0d29273a5acespa
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.keywordDuffy binding proteinspa
dc.subject.keywordcell surfaceeng
dc.subject.keywordHla dr1 antigenspa
dc.subject.keywordHla dr11 antigenspa
dc.subject.keywordHla dr4 antigenspa
dc.subject.keywordHla dr7 antigenspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAntigen bindingspa
dc.subject.keywordArticlespa
dc.subject.keywordBiotinylationspa
dc.subject.keywordControlled studyspa
dc.subject.keywordEnzyme linked immunosorbent assayspa
dc.subject.keywordNucleotide sequencespa
dc.subject.keywordPlasmodium vivaxspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein analysisspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordEpitope mappingspa
dc.subject.keywordHla-dr antigensspa
dc.subject.keywordImmunodominant epitopesspa
dc.subject.keywordMalaria vaccinesspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordPeptidesspa
dc.subject.keywordPlasmodium vivaxspa
dc.subject.keywordProtein conformationspa
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordReceptors, cell surfacespa
dc.subject.keywordSequence alignmentspa
dc.subject.keywordVaccines, syntheticspa
dc.subject.keywordPlasmodium vivaxspa
dc.subject.keywordDuffy binding protein (dbp)spa
dc.subject.keywordMalariaspa
dc.subject.keywordPlasmodium vivaxspa
dc.subject.keywordUniversal epitopesspa
dc.titleIdentification and evaluation of universal epitopes in Plasmodium vivax Duffy binding proteinspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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