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

Gabriela Arévalo-Pinzón, Maritza Bermúdez, Diana Hernández, Hernando Curtidor, Manuel Alfonso Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

5 Citas (Scopus)

Resumen

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.

Idioma originalEnglish (US)
Páginas (desde-hasta)9616
PublicaciónScientific Reports
Volumen7
N.º1
DOI
EstadoPublished - ago 30 2017
Publicado de forma externa

Huella dactilar

Plasmodium vivax
Reticulocytes
Ligands
Antigens
Membranes
Parasites
Erythrocytes
Rosette Formation
Plasmodium
Chymotrypsin
Neuraminidase
Recombinant Proteins
Protein Binding
Proteomics
Proteins
Vaccines
Cell Membrane
Peptides

Citar esto

Arévalo-Pinzón, Gabriela ; Bermúdez, Maritza ; Hernández, Diana ; Curtidor, Hernando ; Patarroyo, Manuel Alfonso. / Plasmodium vivax ligand-receptor interaction : PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+ reticulocytes. En: Scientific Reports. 2017 ; Vol. 7, N.º 1. pp. 9616.
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abstract = "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.",
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Plasmodium vivax ligand-receptor interaction : PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+ reticulocytes. / Arévalo-Pinzón, Gabriela; Bermúdez, Maritza; Hernández, Diana; Curtidor, Hernando; Patarroyo, Manuel Alfonso.

En: Scientific Reports, Vol. 7, N.º 1, 30.08.2017, p. 9616.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Plasmodium vivax ligand-receptor interaction

T2 - PvAMA-1 domain I contains the minimal regions for specific interaction with CD71+ reticulocytes

AU - Arévalo-Pinzón, Gabriela

AU - Bermúdez, Maritza

AU - Hernández, Diana

AU - Curtidor, Hernando

AU - Patarroyo, Manuel Alfonso

PY - 2017/8/30

Y1 - 2017/8/30

N2 - 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.

AB - 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.

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DO - 10.1038/s41598-017-10025-6

M3 - Article

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SP - 9616

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

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ER -