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...
- Autores:
- 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
- Rights
- 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 |
_version_ |
1814167503180398592 |