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

The 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...

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Tipo de recurso:
Fecha de publicación:
2017
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/24942
Acceso en línea:
https://doi.org/10.1038/s41598-017-10025-6
https://repository.urosario.edu.co/handle/10336/24942
Palabra clave:
antígeno de membrana apical-1
candidato a la vacuna contra la malaria
las células rojas de la sangre
proteína de superficie de merozoito-1
ligando de unión a eritrocitos
falciparum merozoitos
parásitos de apicomplexano
expresión condicional
anticuerpo monoclonal
eritrocito huésped
apical membrane antigen-1
malaria vaccine candidate
red-blood-cells
merozoite surface protein-1
erythrocyte-binding ligand
falciparum merozoites
apicomplexan parasites
conditional expression
monoclonal-antibody
host erythrocyte
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License
Abierto (Texto Completo)
id EDOCUR2_f317da25787fe71b0b73a96470de02de
oai_identifier_str oai:repository.urosario.edu.co:10336/24942
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 1a837cee-dfa1-42d9-9f6c-31cbb52d5383-168124dd4-7c85-444d-bcc7-4ed7981b8163-19cf4c90c-9317-4efb-a66a-ed60b6553c1c-191225589-185df39af-db19-401c-a8d0-fcc74ddf550d-12020-06-11T13:21:53Z2020-06-11T13:21:53Z2017The 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.application/pdfhttps://doi.org/10.1038/s41598-017-10025-62045-2322https://repository.urosario.edu.co/handle/10336/24942engNature Publishing Group9616SCIENTIFIC REPORTSVol. 7SCIENTIFIC REPORTS, ISSN:2045-2322, Vol.7, (2017); pp. 9616-Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURantígeno de membrana apical-1candidato a la vacuna contra la malarialas células rojas de la sangreproteína de superficie de merozoito-1ligando de unión a eritrocitosfalciparum merozoitosparásitos de apicomplexanoexpresión condicionalanticuerpo monoclonaleritrocito huéspedapical membrane antigen-1malaria vaccine candidatered-blood-cellsmerozoite surface protein-1erythrocyte-binding ligandfalciparum merozoitesapicomplexan parasitesconditional expressionmonoclonal-antibodyhost erythrocytePlasmodium vivax ligand-receptor interaction: PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+reticulocytesarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Arevalo-Pinzon, GabrielaBermudez, MaritzaHernandez, DianaCurtidor, HernandoAlfonso Patarroyo, Manuel10336/24942oai:repository.urosario.edu.co:10336/249422022-05-02 07:37:21.715708https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Plasmodium vivax ligand-receptor interaction: PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+reticulocytes
title Plasmodium vivax ligand-receptor interaction: PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+reticulocytes
spellingShingle Plasmodium vivax ligand-receptor interaction: PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+reticulocytes
antígeno de membrana apical-1
candidato a la vacuna contra la malaria
las células rojas de la sangre
proteína de superficie de merozoito-1
ligando de unión a eritrocitos
falciparum merozoitos
parásitos de apicomplexano
expresión condicional
anticuerpo monoclonal
eritrocito huésped
apical membrane antigen-1
malaria vaccine candidate
red-blood-cells
merozoite surface protein-1
erythrocyte-binding ligand
falciparum merozoites
apicomplexan parasites
conditional expression
monoclonal-antibody
host erythrocyte
title_short Plasmodium vivax ligand-receptor interaction: PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+reticulocytes
title_full Plasmodium vivax ligand-receptor interaction: PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+reticulocytes
title_fullStr Plasmodium vivax ligand-receptor interaction: PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+reticulocytes
title_full_unstemmed Plasmodium vivax ligand-receptor interaction: PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+reticulocytes
title_sort Plasmodium vivax ligand-receptor interaction: PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+reticulocytes
dc.subject.spa.fl_str_mv antígeno de membrana apical-1
candidato a la vacuna contra la malaria
las células rojas de la sangre
proteína de superficie de merozoito-1
ligando de unión a eritrocitos
falciparum merozoitos
parásitos de apicomplexano
expresión condicional
anticuerpo monoclonal
eritrocito huésped
topic antígeno de membrana apical-1
candidato a la vacuna contra la malaria
las células rojas de la sangre
proteína de superficie de merozoito-1
ligando de unión a eritrocitos
falciparum merozoitos
parásitos de apicomplexano
expresión condicional
anticuerpo monoclonal
eritrocito huésped
apical membrane antigen-1
malaria vaccine candidate
red-blood-cells
merozoite surface protein-1
erythrocyte-binding ligand
falciparum merozoites
apicomplexan parasites
conditional expression
monoclonal-antibody
host erythrocyte
dc.subject.keyword.spa.fl_str_mv apical membrane antigen-1
malaria vaccine candidate
red-blood-cells
merozoite surface protein-1
erythrocyte-binding ligand
falciparum merozoites
apicomplexan parasites
conditional expression
monoclonal-antibody
host erythrocyte
description The 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.
publishDate 2017
dc.date.created.spa.fl_str_mv 2017
dc.date.accessioned.none.fl_str_mv 2020-06-11T13:21:53Z
dc.date.available.none.fl_str_mv 2020-06-11T13:21:53Z
dc.type.eng.fl_str_mv article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_6501
dc.type.spa.spa.fl_str_mv Artículo
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1038/s41598-017-10025-6
dc.identifier.issn.none.fl_str_mv 2045-2322
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/24942
url https://doi.org/10.1038/s41598-017-10025-6
https://repository.urosario.edu.co/handle/10336/24942
identifier_str_mv 2045-2322
dc.language.iso.none.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv
dc.relation.citationStartPage.none.fl_str_mv 9616
dc.relation.citationTitle.none.fl_str_mv SCIENTIFIC REPORTS
dc.relation.citationVolume.none.fl_str_mv Vol. 7
dc.relation.ispartof.spa.fl_str_mv SCIENTIFIC REPORTS, ISSN:2045-2322, Vol.7, (2017); pp. 9616-
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.acceso.spa.fl_str_mv Abierto (Texto Completo)
rights_invalid_str_mv Abierto (Texto Completo)
http://purl.org/coar/access_right/c_abf2
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Nature Publishing Group
institution Universidad del Rosario
dc.source.instname.spa.fl_str_mv instname:Universidad del Rosario
dc.source.reponame.spa.fl_str_mv reponame:Repositorio Institucional EdocUR
repository.name.fl_str_mv Repositorio institucional EdocUR
repository.mail.fl_str_mv edocur@urosario.edu.co
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