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3D structure determination of STARP peptides implicated in P. falciparum invasion of hepatic cells

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dc.creatorBermudez, Adriana
dc.creatorAlba, Martha Patriciaspa
dc.creatorVanegas, Magnoliaspa
dc.creatorPatarroyo, Manuel Elkinspa
dc.date.accessioned2020-05-26T00:02:12Z
dc.date.available2020-05-26T00:02:12Z
dc.date.created2010spa
dc.description.abstractTo block the different stages of Plasmodium falciparum invasion into human hepatocytes and red blood cells, we have focused on those proteins belonging to the pre-erythrocytic stage. One of these proteins is Sporozoite Threonine and Asparagine Rich Protein (STARP), which is a ligand used by P. falciparum parasites to bind Hepatic cells (HepG2). Previous studies on this protein identified two conserved peptides binding with high activity to HepG2 cells (namely 20546 and 20570) with corresponding critical hepatic-cell binding residues and determined an important role for these two peptides in the invasion process. This study shows the results of immunization trials in Aotus monkeys with native STARP peptides and analogues modified in critical hepatic-cell binding residues. The results show that native peptides are not immunogenic but can induce high-antibody titers when their critical residues are replaced by other with similar volume and mass but different polarity. Nuclear Magnetic Resonance (1H NMR) studies revealed that native peptides (non-immunogenic) displayed shorter ?-helical regions compared to their highly immunogenic modified analogues. Binding assays with HLA-DR?1* molecules showed that 20546 modified peptides inducing high-antibody titers (24972, 24320 and 24486) bound to HLA-DR?1*0301 molecules, while the 20570 modified analogue (24322) bound to HLA-DR?1*0101. The results support including these high-immunogenic STARP-derived modified peptides as pre-erythrocytic candidates to be included in the design of a synthetic antimalarial vaccine. © 2010 Elsevier Ltd.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.vaccine.2010.05.025
dc.identifier.issn0264410X
dc.identifier.issn13588745
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23458
dc.language.isoengspa
dc.relation.citationEndPage4996
dc.relation.citationIssueNo. 31
dc.relation.citationStartPage4989
dc.relation.citationTitleVaccine
dc.relation.citationVolumeVol. 28
dc.relation.ispartofVaccine, ISSN:0264410X, 13588745, Vol.28, No.31 (2010); pp. 4989-4996spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77954758555&doi=10.1016%2fj.vaccine.2010.05.025&partnerID=40&md5=68f60d83b0a521fdd15ad37c00acc47cspa
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.keywordHLA DQB1 antigenspa
dc.subject.keywordFalciparumeng
dc.subject.keywordProtozoal proteinspa
dc.subject.keywordSporozoite threonine and asparagine rich proteinspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordHLA DR antigenspa
dc.subject.keywordHLA DRB1 antigenspa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordParasite antigenspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtozoon antibodyspa
dc.subject.keywordSTARP antigeneng
dc.subject.keywordAlpha helixspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimal experimentspa
dc.subject.keywordAnimal modelspa
dc.subject.keywordAotusspa
dc.subject.keywordArticlespa
dc.subject.keywordCircular dichroismspa
dc.subject.keywordControlled studyspa
dc.subject.keywordDrug structurespa
dc.subject.keywordImmunogenicityspa
dc.subject.keywordNonhumanspa
dc.subject.keywordNuclear Overhauser effectspa
dc.subject.keywordPeptide synthesisspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProton nuclear magnetic resonancespa
dc.subject.keywordSporozoitespa
dc.subject.keywordVaccine productionspa
dc.subject.keywordAnimalspa
dc.subject.keywordAntibody productionspa
dc.subject.keywordBloodspa
dc.subject.keywordChemistryspa
dc.subject.keywordHumanspa
dc.subject.keywordImmunologyspa
dc.subject.keywordLiver cellspa
dc.subject.keywordMalaria falciparumspa
dc.subject.keywordMolecular geneticsspa
dc.subject.keywordParasitologyspa
dc.subject.keywordPathogenicityspa
dc.subject.keywordProtein tertiary structurespa
dc.subject.keywordAmino Acid Sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordAntibodieseng
dc.subject.keywordAntibody Formationspa
dc.subject.keywordAntigenseng
dc.subject.keywordAotus trivirgatusspa
dc.subject.keywordHepatocytesspa
dc.subject.keywordHLA-DR Antigensspa
dc.subject.keywordHumansspa
dc.subject.keywordMalaria Vaccinesspa
dc.subject.keywordMalariaeng
dc.subject.keywordMolecular Sequence Dataspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein Bindingspa
dc.subject.keywordProtein Structureeng
dc.subject.keywordAmino Acid Sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordAntibodieseng
dc.subject.keywordAntibody Formationspa
dc.subject.keywordAntigenseng
dc.subject.keywordAotus trivirgatusspa
dc.subject.keywordHepatocytesspa
dc.subject.keywordHLA-DR Antigensspa
dc.subject.keywordHLA-DRB1 Chainsspa
dc.subject.keywordHumansspa
dc.subject.keywordMalaria Vaccinesspa
dc.subject.keywordMalariaeng
dc.subject.keywordMolecular Sequence Dataspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein Bindingspa
dc.subject.keywordProtein Structureeng
dc.subject.keyword1H NMRspa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordSporozoitespa
dc.subject.keywordStructurespa
dc.title3D structure determination of STARP peptides implicated in P. falciparum invasion of hepatic cellsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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