Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion

Hernando Curtidor, Liliana C. Patiño, Gabriela Arévalo-Pinzón, Magnolia Vanegas, Manuel E. Patarroyo, Manuel A. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

6 Citas (Scopus)

Resumen

Plasmodium falciparum malaria parasite invasion of erythrocytes is an essential step in host infection and the proteins involved in such invasion are the main target in developing an antimalarial vaccine. Secretory organelle-derived proteins (micronemal AMA1 protein and the RON2, 4, and 5 rhoptry neck proteins) have been recently described as components of moving junction complex formation allowing merozoites to move into a newly created parasitophorous vacuole. This study led to identifying RON5 regions involved in binding to human erythrocytes by using a highly robust, sensitive and specific receptor-ligand interaction assay; it is further shown that the RON5 protein remains highly conserved throughout different parasite strains. It is shown that the binding peptide-erythrocyte interaction is saturable and sensitive to chymotrypsin and trypsin. Invasion inhibition assays using erythrocyte binding peptides showed that the RON5-erythrocyte interaction could be critical for merozoite invasion of erythrocytes. This work provides evidence (for the first time) suggesting a fundamental role for RON5 in erythrocyte invasion. © 2013 Elsevier Inc.
Idioma originalEnglish (US)
Páginas (desde-hasta)210-217
Número de páginas8
PublicaciónPeptides
DOI
EstadoPublished - ene 1 2014

Huella dactilar

Plasmodium falciparum
Parasites
Blood
Neck
Erythrocytes
Cells
Peptides
Proteins
Merozoites
Assays
Antimalarials
Falciparum Malaria
Vaccines
Vacuoles
Ligands
Organelles
Infection

Citar esto

Curtidor, Hernando ; Patiño, Liliana C. ; Arévalo-Pinzón, Gabriela ; Vanegas, Magnolia ; Patarroyo, Manuel E. ; Patarroyo, Manuel A. / Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion. En: Peptides. 2014 ; pp. 210-217.
@article{97d27524da994655bf0c6c257002adf1,
title = "Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion",
abstract = "Plasmodium falciparum malaria parasite invasion of erythrocytes is an essential step in host infection and the proteins involved in such invasion are the main target in developing an antimalarial vaccine. Secretory organelle-derived proteins (micronemal AMA1 protein and the RON2, 4, and 5 rhoptry neck proteins) have been recently described as components of moving junction complex formation allowing merozoites to move into a newly created parasitophorous vacuole. This study led to identifying RON5 regions involved in binding to human erythrocytes by using a highly robust, sensitive and specific receptor-ligand interaction assay; it is further shown that the RON5 protein remains highly conserved throughout different parasite strains. It is shown that the binding peptide-erythrocyte interaction is saturable and sensitive to chymotrypsin and trypsin. Invasion inhibition assays using erythrocyte binding peptides showed that the RON5-erythrocyte interaction could be critical for merozoite invasion of erythrocytes. This work provides evidence (for the first time) suggesting a fundamental role for RON5 in erythrocyte invasion. {\circledC} 2013 Elsevier Inc.",
author = "Hernando Curtidor and Pati{\~n}o, {Liliana C.} and Gabriela Ar{\'e}valo-Pinz{\'o}n and Magnolia Vanegas and Patarroyo, {Manuel E.} and Patarroyo, {Manuel A.}",
year = "2014",
month = "1",
day = "1",
doi = "10.1016/j.peptides.2013.07.028",
language = "English (US)",
pages = "210--217",
journal = "Peptides",
issn = "0196-9781",
publisher = "Elsevier Inc.",

}

Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion. / Curtidor, Hernando; Patiño, Liliana C.; Arévalo-Pinzón, Gabriela; Vanegas, Magnolia; Patarroyo, Manuel E.; Patarroyo, Manuel A.

En: Peptides, 01.01.2014, p. 210-217.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion

AU - Curtidor, Hernando

AU - Patiño, Liliana C.

AU - Arévalo-Pinzón, Gabriela

AU - Vanegas, Magnolia

AU - Patarroyo, Manuel E.

AU - Patarroyo, Manuel A.

PY - 2014/1/1

Y1 - 2014/1/1

N2 - Plasmodium falciparum malaria parasite invasion of erythrocytes is an essential step in host infection and the proteins involved in such invasion are the main target in developing an antimalarial vaccine. Secretory organelle-derived proteins (micronemal AMA1 protein and the RON2, 4, and 5 rhoptry neck proteins) have been recently described as components of moving junction complex formation allowing merozoites to move into a newly created parasitophorous vacuole. This study led to identifying RON5 regions involved in binding to human erythrocytes by using a highly robust, sensitive and specific receptor-ligand interaction assay; it is further shown that the RON5 protein remains highly conserved throughout different parasite strains. It is shown that the binding peptide-erythrocyte interaction is saturable and sensitive to chymotrypsin and trypsin. Invasion inhibition assays using erythrocyte binding peptides showed that the RON5-erythrocyte interaction could be critical for merozoite invasion of erythrocytes. This work provides evidence (for the first time) suggesting a fundamental role for RON5 in erythrocyte invasion. © 2013 Elsevier Inc.

AB - Plasmodium falciparum malaria parasite invasion of erythrocytes is an essential step in host infection and the proteins involved in such invasion are the main target in developing an antimalarial vaccine. Secretory organelle-derived proteins (micronemal AMA1 protein and the RON2, 4, and 5 rhoptry neck proteins) have been recently described as components of moving junction complex formation allowing merozoites to move into a newly created parasitophorous vacuole. This study led to identifying RON5 regions involved in binding to human erythrocytes by using a highly robust, sensitive and specific receptor-ligand interaction assay; it is further shown that the RON5 protein remains highly conserved throughout different parasite strains. It is shown that the binding peptide-erythrocyte interaction is saturable and sensitive to chymotrypsin and trypsin. Invasion inhibition assays using erythrocyte binding peptides showed that the RON5-erythrocyte interaction could be critical for merozoite invasion of erythrocytes. This work provides evidence (for the first time) suggesting a fundamental role for RON5 in erythrocyte invasion. © 2013 Elsevier Inc.

U2 - 10.1016/j.peptides.2013.07.028

DO - 10.1016/j.peptides.2013.07.028

M3 - Article

C2 - 23932940

SP - 210

EP - 217

JO - Peptides

JF - Peptides

SN - 0196-9781

ER -