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Plasmodium vivax ligand-receptor interaction : PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+ reticulocytes

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dc.creatorArévalo-Pinzón, Gabriela
dc.creatorBermúdez, Maritza
dc.creatorHernández, Diana
dc.creatorCurtidor, Hernando
dc.creatorPatarroyo, Manuel A.
dc.creator.googleArévalo-Pinzón, Gabrielaspa
dc.creator.googleBermúdez, Maritzaspa
dc.creator.googleHernández, Dianaspa
dc.creator.googleCurtidor, Hernandospa
dc.creator.googlePatarroyo, Manuel Alfonsospa
dc.date.accessioned2019-01-28T17:17:14Z
dc.date.available2019-01-28T17:17:14Z
dc.date.created2017
dc.date.issued2017
dc.description.abstractThe malarial parasite's invasion is complex, active and coordinated, involving many low and high affinity interactions with receptors on target cell membrane. Proteomics analysis has described around 40 proteins in P. vivax which could be involved in reticulocyte invasion; few have been studied with the aim of elucidating how many of them establish specific interactions with their respective host cells. Given the importance of knowing which of the parasite's protein regions are functionally important for invasion, minimum regions mediating specific interaction between Plasmodium vivax apical membrane antigen 1 (PvAMA-1) and its host cell were here elucidated. The region covering PvAMA-1 domains I and II (PvAMA-DI-II) specifically bound to the CD71+ red blood cell subpopulation. A 20 residue-long region (81EVENAKYRIPAGRCPVFGKG100) located in domain I was capable of inhibiting PvAMA-DI-II recombinant protein binding to young reticulocytes (CD71+CD45-) and rosette formation. This conserved peptide specifically interacted with high affinity with reticulocytes (CD71+) through a neuraminidase-and chymotrypsin-treatment sensitive receptor. Such results showed that, despite AMA-1 having universal functions during late Plasmodium invasion stages, PvAMA-1 had reticulocyte-preferring binding regions, suggesting that P. vivax target cell selection is not just restricted to initial interactions but maintained throughout the erythrocyte invasion cycle, having important implications for designing a specific anti-P. vivax vaccine. © 2017 The Author(s).eng
dc.format.mimetypeapplication/pdf
dc.identifier.issnISSN 2045-2322
dc.identifier.urihttp://repository.urosario.edu.co/handle/10336/18941
dc.language.isoengspa
dc.relation.citationIssueNo. 1
dc.relation.citationTitleScientific Reports
dc.relation.citationVolumeVol. 7
dc.relation.ispartofScientific Reports, ISSN: 2045-2322, Vol. 7/No. 1 (2017)spa
dc.relation.urihttps://www.nature.com/articles/s41598-017-10025-6.pdfspa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.rights.cchttp://creativecommons.org/licenses/by/4.0/spa
dc.source.bibliographicCitationGething, P.W., A long neglected world malaria map: Plasmodium vivax endemicity in 2010 (2012) PLoS Negl Trop Dis, 6, p. e1814spa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subjectPlasmodium vivaxspa
dc.subjectMalariaspa
dc.subject.ddcEnfermedadesspa
dc.subject.lembPlasmodium vivaxspa
dc.subject.lembMalariaspa
dc.titlePlasmodium vivax ligand-receptor interaction : PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+ reticulocytesspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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