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Identification of Plasmodium falciparum RhopH3 protein peptides that specifically bind to erythrocytes and inhibit merozoite invasion

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dc.creatorPinzón, Carlos Giovannispa
dc.creatorCurtidor, Hernandospa
dc.creatorReyes, Claudiaspa
dc.creatorMéndez, Davidspa
dc.creatorPatarroyo, Manuel Elkinspa
dc.date.accessioned2020-05-25T23:58:35Z
dc.date.available2020-05-25T23:58:35Z
dc.date.created2008spa
dc.description.abstractThe identification of sequences involved in binding to erythrocytes is an important step for understanding the molecular basis of merozoite-erythrocyte interactions that take place during invasion of the Plasmodium falciparum malaria parasite into host cells. Several molecules located in the apical organelles (micronemes, rhoptry, dense granules) of the invasive-stage parasite are essential for erythrocyte recognition, invasion, and establishment of the nascent parasitophorous vacuole. Particularly, it has been demonstrated that rhoptry proteins play an important role in binding to erythrocyte surface receptors, among which is the Pf RhopH3 protein, which triggers important immune responses in patients from endemic regions. It has also been reported that anti-RhopH3 antibodies inhibit in vitro invasion of erythrocytes, further supporting its direct involvement in erythrocyte invasion processes. In this study, Pf RhopH3 consecutive peptides were synthesized and tested in erythrocyte binding assays for identifying those regions mediating binding to erythrocytes. Fourteen Pf RhopH3 peptides presenting high specific binding activity were found, whose bindings were saturable and presented nanomolar dissociation constants. These high-activity binding peptides (HABPs) were characterized by having a-helical structural elements, as determined by circular dichroism, and having receptors of a possible sialic acid-dependent and/or glycoprotein- dependent nature, as evidenced in enzyme-treated erythrocyte binding assays and further corroborated by cross-linking assay results. Furthermore, these HABPs inhibited merozoite in vitro invasion of normal erythrocytes at 200 mM by up to 60% and 90%, suggesting that some RhopH3 protein regions are involved in the P. falciparum erythrocyte invasion. Copyright © 2008 The Protein Society.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1110/ps.035923.108
dc.identifier.issn9618368
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22892
dc.language.isoengspa
dc.relation.citationEndPage1730
dc.relation.citationIssueNo. 10
dc.relation.citationStartPage1719
dc.relation.citationTitleProtein Science
dc.relation.citationVolumeVol. 17
dc.relation.ispartofProtein Science, ISSN:9618368, Vol.17, No.10 (2008); pp. 1719-1730spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-52949123658&doi=10.1110%2fps.035923.108&partnerID=40&md5=f6fbba220d5a08efdeee9c6a2558c008spa
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.keywordProtein rhoph3spa
dc.subject.keywordProtozoal proteinspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordBinding assayspa
dc.subject.keywordCell interactionspa
dc.subject.keywordCell invasionspa
dc.subject.keywordErythrocytespa
dc.subject.keywordErythrocyte membranespa
dc.subject.keywordHost parasite interactionspa
dc.subject.keywordImmune responsespa
dc.subject.keywordMerozoitespa
dc.subject.keywordNonhumanspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein functionspa
dc.subject.keywordReceptor bindingspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordBinding sitesspa
dc.subject.keywordErythrocytesspa
dc.subject.keywordHumansspa
dc.subject.keywordMalaria vaccinesspa
dc.subject.keywordMerozoitesspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordPeptide fragmentsspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein conformationspa
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordTrypsinspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordHigh-activity binding peptidesspa
dc.subject.keywordMalariaspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordRhoph3 proteinspa
dc.titleIdentification of Plasmodium falciparum RhopH3 protein peptides that specifically bind to erythrocytes and inhibit merozoite invasionspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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