Ítem
Acceso Abierto

Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion

Mostrar el registro sencillo de la publicación
dc.creatorArévalo-Pinzón, Gabrielaspa
dc.creatorCurtidor, Hernandospa
dc.creatorMuñoz, Marinaspa
dc.creatorSuarez, Dianaspa
dc.creatorPatarroyo, Manuel A.spa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-05-26T00:02:13Z
dc.date.available2020-05-26T00:02:13Z
dc.date.created2013spa
dc.description.abstractIdentifying the minimal functional regions of the proteins which the malaria parasite uses when invading its host cells constitutes the first and most important approach in an effective design for a chemically synthesised, multi-antigen, multi-stage, subunit-based vaccine. This work has been aimed at identifying the PfRh1 protein binding regions (residues 1-2580) belonging to the reticulocyte binding-like (RBL or P. falciparum Rh [PfRh]) family implicated in the parasite's alternative target cell invasion routes. Eighteen peptide regions (called high activity binding peptides - HABPs) binding to red blood cells (RBC) were identified in peptides mapped in a highly robust, specific and sensitive receptor-ligand assay. These HABPs were saturable in the experimental conditions assayed here and most had an alpha helix structure. Polymorphism studies revealed that only six of the eighteen HABPs identified had changes at amino acid level amongst the seven P. falciparum strains evaluated. Most HABPs' specific binding became altered when RBC were treated with neuraminidase, chymotrypsin and trypsin, suggesting differing sensitivity for RBC membrane receptors. After ascertaining that the Rh1 gene was transcribed and expressed in late-stage schizonts of the FCB-2 strain, invasion inhibition assays were carried out. When most of these HABPs were assayed in P. falciparum in vitro culture they were able to inhibit high percentages of FVO strain invasion compared to low inhibition percentages observed with the FCB-2 strain. This data shows small Rh1 regions' participation during invasion and suggests that these units should be included in further immunological and structural studies. © 2013 Elsevier Ltd.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.vaccine.2013.01.052
dc.identifier.issn0264410X
dc.identifier.issn13588745
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23460
dc.language.isoengspa
dc.relation.citationEndPage1837
dc.relation.citationIssueNo. 14
dc.relation.citationStartPage1830
dc.relation.citationTitleVaccine
dc.relation.citationVolumeVol. 31
dc.relation.ispartofVaccine, ISSN:0264410X, 13588745, Vol.31, No.14 (2013); pp. 1830-1837spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84875262025&doi=10.1016%2fj.vaccine.2013.01.052&partnerID=40&md5=311561ae13a870b5a99facbc23290097spa
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.keywordAmino acidspa
dc.subject.keywordMembrane receptorspa
dc.subject.keywordProteinspa
dc.subject.keywordRh1 proteinspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAlpha helixspa
dc.subject.keywordArticlespa
dc.subject.keywordCell invasionspa
dc.subject.keywordControlled studyspa
dc.subject.keywordErythrocytespa
dc.subject.keywordGene expressionspa
dc.subject.keywordIn vitro studyspa
dc.subject.keywordNonhumanspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein polymorphismspa
dc.subject.keywordReticulocytespa
dc.subject.keywordSchizontspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordErythrocytesspa
dc.subject.keywordHost-pathogen interactionsspa
dc.subject.keywordHumansspa
dc.subject.keywordMalariaspa
dc.subject.keywordMalaria vaccinesspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordPeptidesspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein structure, secondaryspa
dc.subject.keywordProtein structure, tertiaryspa
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordSchizontsspa
dc.subject.keywordVaccineseng
dc.subject.keywordMalariaspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordReticulocyte binding-likespa
dc.subject.keywordSynthetic peptidespa
dc.titleRh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasionspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
Archivos
Bloque original
Mostrando1 - 1 de 1
Miniatura
Nombre:
Rh1_high_activity_binding_peptides_inhib.pdf
Tamaño:
773.73 KB
Formato:
Adobe Portable Document Format
Descripción:
Descargar
Colecciones
Artículos