Ítem
Solo Metadatos

Identifying Plasmodium falciparum merozoite surface protein-10 human erythrocyte specific binding regions

Mostrar el registro sencillo de la publicación
dc.creatorPuentes, Alvarospa
dc.creatorOcampo, Marisolspa
dc.creatorRodríguez, Luis Eduardospa
dc.creatorVera, Ricardospa
dc.creatorValbuena, Johnspa
dc.creatorCurtidor, Hernandospa
dc.creatorGarcía, Javierspa
dc.creatorLópez, Ramsésspa
dc.creatorTovar, Dianaspa
dc.creatorCortes, Jimenaspa
dc.creatorRivera, Zulyspa
dc.creatorPatarroyo, Manuel Elkinspa
dc.date.accessioned2020-08-06T16:20:22Z
dc.date.available2020-08-06T16:20:22Z
dc.date.created2005-05spa
dc.description.abstractReceptor-ligand interactions between synthetic peptides and normal human erythrocytes were studied to determine P. falciparum merozoite surface protein-10 (MSP-10) regions specifically binding to membrane surface receptors on human erythrocytes. Three MSP-10 protein High Activity Binding Peptides (HABPs) were identified, whose binding to erythrocytes became saturable and sensitive on being treated with neuraminidase, trypsin and chymotrypsin. Some of them specifically recognised a 50 kDa erythrocyte membrane protein. Some HABPs inhibited in vitro P. falciparum merozoite invasion of erythrocytes by 70%, suggesting that MSP-10 protein’s possible role in the invasion process probably functions by using similar mechanisms to those described for other MSP family antigens. In addition to above results, the high homology in amino-acid sequence and superimposition of both MSP-10, MSP-8 and MSP-1 EGF-like domains and HABPs 31132, 26373 and 5501 suggest that tridimensional structure could be playing an important role in the invasion process and in designing synthetic multi-stage anti-malarial vaccines.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.biochi.2005.01.001
dc.identifier.issnISSN: 0300-9084
dc.identifier.issnEISSN: 6183-1638
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/25975
dc.language.isoengspa
dc.publisherElsevierspa
dc.relation.citationEndPage472
dc.relation.citationIssueNo. 5
dc.relation.citationStartPage461
dc.relation.citationTitleBiochimie
dc.relation.citationVolumeVol. 87
dc.relation.ispartofBiochimie, ISSN: 0300-9084;EISSN: 6183-1638, Vol.87 No.5 (2005); pp.461-472spa
dc.relation.urihttps://www.sciencedirect.com/science/article/abs/pii/S030090840500spa
dc.rights.accesRightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.accesoRestringido (Acceso a grupos específicos)spa
dc.sourceBiochimiespa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subject.keywordP. falciparumspa
dc.subject.keywordMerozoite surface protein 10spa
dc.subject.keywordMSP-10spa
dc.subject.keywordHigh activity bindingspa
dc.subject.keywordPeptidesspa
dc.subject.keywordInvasion inhibitionspa
dc.titleIdentifying Plasmodium falciparum merozoite surface protein-10 human erythrocyte specific binding regionsspa
dc.title.TranslatedTitleIdentificación de Plasmodium falciparum merozoito superficie proteína-10 regiones de unión específica de eritrocitos humanosspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
Archivos
Colecciones
Artículos