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P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro

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dc.creatorValbuena, Johnspa
dc.creatorVera, Ricardospa
dc.creatorPuentes, Alvarospa
dc.creatorOcampo, Marisol
dc.creatorGarcia, Javierspa
dc.creatorCurtidor, Hernandospa
dc.creatorLopez, Ramsesspa
dc.creatorRodríguez, Luis
dc.creatorRosas, Jaiverspa
dc.creatorCortes, Jimenaspa
dc.creatorForero, Marthaspa
dc.creatorPinto, Marthaspa
dc.creatorPatarroyo, Manuel Elkinspa
dc.date.accessioned2020-08-19T14:40:02Z
dc.date.available2020-08-19T14:40:02Z
dc.date.created2005-07-05spa
dc.description.abstractPlasmodium falciparum histoaspartic protease (HAP) is an active enzyme involved in haemoglobin degradation. HAP is expressed as an inactive 51-kDa zymogen and is cleaved into an active 37-kDa enzyme. It has been proposed that this kind of protease might be implicated in the parasite's invasion of erythrocytes; however, this protein's role during invasion has still to be determined. Synthetic peptides derived from the HAP precursor (proHAP) were tested in erythrocyte binding assays to identify their possible function in the invasion process. Two proHAP high-activity binding peptides (HABPs) specifically bound to erythrocytes; these peptides were numbered 30609 (101LKNYIKESVKLFNKGLTKKS120) and 30610 (121YLGSEFDNVELKDLANVLSF140). The binding of these two peptides was saturable, presenting nanomolar affinity constants. These peptides interacted with 26- and 45-kDa proteins on the erythrocyte surface; the nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. The HABPs showed greater than 90% merozoite invasion inhibition in in vitro assays. Goat serum containing proHAP polymeric peptide antibodies inhibited parasite invasion in vitro.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1515/BC.2005.043
dc.identifier.issnISSN: 1431-6730
dc.identifier.issnEISSN: 1437-4315
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/26682
dc.language.isoengspa
dc.publisherWalter de Gruyterspa
dc.relation.citationEndPage367
dc.relation.citationIssueNo. 4
dc.relation.citationStartPage361
dc.relation.citationTitleBiological Chemistry
dc.relation.citationVolumeVol. 386
dc.relation.ispartofBiological Chemistry, ISSN: 1431-6730;EISSN: 1437-4315, Vol.386, No.4 (April 2005); pp. 361-367spa
dc.relation.urihttps://www.degruyter.com/view/journals/bchm/386/4/article-p361.xmlspa
dc.rights.accesRightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.accesoRestringido (Acceso a grupos específicos)spa
dc.sourceBiological Chemistryspa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subject.keywordBinding assayspa
dc.subject.keywordMalariaspa
dc.subject.keywordProteasespa
dc.subject.keywordSynthetic peptidespa
dc.titleP. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitrospa
dc.title.TranslatedTitleLos péptidos de la proteína proteasa pro-histoaspártica (proHAP) de P. falciparum se unen específicamente a los eritrocitos e inhiben el proceso de invasión in vitroeng
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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