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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.creatorArevalo-Pinzon, Gabrielaspa
dc.creatorBermudez, Maritzaspa
dc.creatorHernandez, Dianaspa
dc.creatorCurtidor, Hernandospa
dc.creatorAlfonso Patarroyo, Manuelspa
dc.date.accessioned2020-06-11T13:21:53Z
dc.date.available2020-06-11T13:21:53Z
dc.date.created2017spa
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 ((81)EVENAKYRIPAGRCPVFGKG(100)) 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.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1038/s41598-017-10025-6
dc.identifier.issn2045-2322
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/24942
dc.language.isoeng
dc.publisherNature Publishing Groupspa
dc.relation.citationEndPage
dc.relation.citationStartPage9616
dc.relation.citationTitleSCIENTIFIC REPORTS
dc.relation.citationVolumeVol. 7
dc.relation.ispartofSCIENTIFIC REPORTS, ISSN:2045-2322, Vol.7, (2017); pp. 9616-spa
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.subjectantígeno de membrana apical-1spa
dc.subjectcandidato a la vacuna contra la malariaspa
dc.subjectlas células rojas de la sangrespa
dc.subjectproteína de superficie de merozoito-1spa
dc.subjectligando de unión a eritrocitosspa
dc.subjectfalciparum merozoitosspa
dc.subjectparásitos de apicomplexanospa
dc.subjectexpresión condicionalspa
dc.subjectanticuerpo monoclonalspa
dc.subjecteritrocito huéspedspa
dc.subject.keywordapical membrane antigen-1spa
dc.subject.keywordmalaria vaccine candidatespa
dc.subject.keywordred-blood-cellsspa
dc.subject.keywordmerozoite surface protein-1spa
dc.subject.keyworderythrocyte-binding ligandspa
dc.subject.keywordfalciparum merozoitesspa
dc.subject.keywordapicomplexan parasitesspa
dc.subject.keywordconditional expressionspa
dc.subject.keywordmonoclonal-antibodyspa
dc.subject.keywordhost erythrocytespa
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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