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Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells

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dc.creatorGarcía, Javier E.spa
dc.creatorPuentes, Alvarospa
dc.creatorCurtidor, Hernandospa
dc.creatorVera, Ricardospa
dc.creatorRodríguez, Luis
dc.creatorValbuena, Johnspa
dc.creatorLópez, Ramsesspa
dc.creatorOcampo, Marisol
dc.creatorCortés, Jimenaspa
dc.creatorVanegas, Magnoliaspa
dc.creatorRosas, Jaiverspa
dc.creatorReyes, Claudiaspa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-08-19T14:40:05Z
dc.date.available2020-08-19T14:40:05Z
dc.date.created2005-07-01spa
dc.description.abstractSynthetic 20-mer long non-overlapped peptides, from STEVOR protein, were tested in RBC binding assays for identifying STEVOR protein regions having high RBC binding activity and evaluating whether these regions inhibit Plasmodium falciparum in vitro invasion. Affinity constants, binding site number per cell and Hill coefficients were determined by saturation assay with high activity binding peptides (HABPs). HABP binding assays using RBCs previously treated with enzymes were carried out to study the nature of the receptor. The molecular weight of RBC surface proteins interacting with HABPs was determined by cross-linking assays and SDS-PAGE analysis. RBC binding assays revealed that peptides 30561 (41MKSRRLAEIQLPKCPHYNND60), 30562 (61PELKKIIDKLNEERIKKYIE80) and 30567 (161ASCCKVHDNYLDNLKKGCFG180) bound saturably and with high binding activity, presenting nanomolar affinity constants. HABP binding activity to RBCs previously treated with neuraminidase and trypsin decreased, suggesting that these peptides bound to RBC surface proteins and that such binding could be sialic acid dependent. Cross-linking and SDS-PAGE assays showed that the three HABPs specifically bound to 30 and 40 kDa molecular weight RBC membrane proteins. Peptides 30561, 30562 and 30567 inhibited P. falciparum in vitro invasion of red blood cells in a concentration-dependent way. Goat sera having STEVOR protein polymeric peptides antibodies inhibit parasite in vitro invasion depending on concentration. Three peptides localized in STEVOR N-terminal and central regions had high, saturable, binding activity to 30 and 40 kDa RBC membrane proteins. These peptides inhibited the parasite's in vitro invasion, suggesting that STEVOR protein regions are involved in P. falciparum invasion processes during intra-erythrocyte stage.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.peptides.2005.01.013
dc.identifier.issnISSN: 0196-9781
dc.identifier.issnEISSN: 1873-5169
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/26703
dc.language.isoengspa
dc.publisherElsevierspa
dc.relation.citationEndPage1143
dc.relation.citationIssueNo. 7
dc.relation.citationStartPage1133
dc.relation.citationTitlePeptides
dc.relation.citationVolumeVol. 26
dc.relation.ispartofPeptides, ISSN: 0196-9781;EISSN: 1873-5169, Vol.26, No.7 (2005); pp. 1133-1143spa
dc.relation.urihttps://www.sciencedirect.com/science/article/abs/pii/S0196978105000276spa
dc.rights.accesRightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.accesoRestringido (Acceso a grupos específicos)spa
dc.sourcePeptidesspa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subject.keywordP. falciparumspa
dc.subject.keywordSTEVORspa
dc.subject.keywordHigh activity binding peptidesspa
dc.titlePeptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cellsspa
dc.title.alternativePeptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cellsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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