Conserved high activity binding peptides from the Plasmodium falciparum Pf34 rhoptry protein inhibit merozoites in vitro invasion of red blood cells

Gabriela Arévalo-Pinzón, Hernando Curtidor, Magnolia Vanegas, Carolina Vizcaíno, Manuel A. Patarroyo, Manuel E. Patarroyo

Resultado de la investigación: Contribución a una revistaArtículo

10 Citas (Scopus)

Resumen

Rhoptries are specialized secretory organelles found in all members of the genus Plasmodium whose proteins have been considered as promising vaccine candidates due to their involvement in cell invasion and the formation of the parasitophorous vacuole (PV). The Plasmodium falciparum Pf34 protein was recently identified as a rhoptry-neck protein located in detergent-resistant microdomains (DRMs) that is expressed in mature intraerythrocytic parasite stages, but its biological function is still unknown. Receptor-ligand assays carried out in this study found that peptides 36,051 ( 101DKKFSESLKAHMDHLKILNN120Y), 36,053 ( 141KKYIIKEIQNNKYLNKEKKS160), 36,055 ( 181WLESVNNIEEKSNILKNIKS200Y) and 36,056 ( 201QLLNNIASLNHTLSEEIKNI220Y), located in the central portion of Pf34, were found to establish protease-sensitive interactions of high affinity and specificity with receptors on the surface of red blood cell (RBCs). In vitro assays showed that Pf34 high activity binding peptides (HABPs) inhibit invasion of RBCs by P. falciparum merozoites, therefore suggesting that Pf34 could act as an adhesin during invasion and supporting the inclusion of Pf34 HABPs in further studies to develop antimalarial control methods. © 2010 Elsevier Inc. All rights reserved.
Idioma originalInglés estadounidense
Páginas (desde-hasta)1987-1994
Número de páginas8
PublicaciónPeptides
DOI
EstadoPublicada - nov 1 2010

Huella dactilar

Merozoites
Blood
Erythrocytes
Cells
Peptides
Assays
Proteins
Plasmodium
Antimalarials
Plasmodium falciparum
Vacuoles
Organelles
Detergents
Parasites
Peptide Hydrolases
Neck
Vaccines
Ligands
Plasmodium falciparum Pf34 protein
In Vitro Techniques

Citar esto

Arévalo-Pinzón, Gabriela ; Curtidor, Hernando ; Vanegas, Magnolia ; Vizcaíno, Carolina ; Patarroyo, Manuel A. ; Patarroyo, Manuel E. / Conserved high activity binding peptides from the Plasmodium falciparum Pf34 rhoptry protein inhibit merozoites in vitro invasion of red blood cells. En: Peptides. 2010 ; pp. 1987-1994.
@article{786c916b06214d73894f7247b006fced,
title = "Conserved high activity binding peptides from the Plasmodium falciparum Pf34 rhoptry protein inhibit merozoites in vitro invasion of red blood cells",
abstract = "Rhoptries are specialized secretory organelles found in all members of the genus Plasmodium whose proteins have been considered as promising vaccine candidates due to their involvement in cell invasion and the formation of the parasitophorous vacuole (PV). The Plasmodium falciparum Pf34 protein was recently identified as a rhoptry-neck protein located in detergent-resistant microdomains (DRMs) that is expressed in mature intraerythrocytic parasite stages, but its biological function is still unknown. Receptor-ligand assays carried out in this study found that peptides 36,051 ( 101DKKFSESLKAHMDHLKILNN120Y), 36,053 ( 141KKYIIKEIQNNKYLNKEKKS160), 36,055 ( 181WLESVNNIEEKSNILKNIKS200Y) and 36,056 ( 201QLLNNIASLNHTLSEEIKNI220Y), located in the central portion of Pf34, were found to establish protease-sensitive interactions of high affinity and specificity with receptors on the surface of red blood cell (RBCs). In vitro assays showed that Pf34 high activity binding peptides (HABPs) inhibit invasion of RBCs by P. falciparum merozoites, therefore suggesting that Pf34 could act as an adhesin during invasion and supporting the inclusion of Pf34 HABPs in further studies to develop antimalarial control methods. {\circledC} 2010 Elsevier Inc. All rights reserved.",
author = "Gabriela Ar{\'e}valo-Pinz{\'o}n and Hernando Curtidor and Magnolia Vanegas and Carolina Vizca{\'i}no and Patarroyo, {Manuel A.} and Patarroyo, {Manuel E.}",
year = "2010",
month = "11",
day = "1",
doi = "10.1016/j.peptides.2010.07.009",
language = "English (US)",
pages = "1987--1994",
journal = "Peptides",
issn = "0196-9781",
publisher = "Elsevier Inc.",

}

Conserved high activity binding peptides from the Plasmodium falciparum Pf34 rhoptry protein inhibit merozoites in vitro invasion of red blood cells. / Arévalo-Pinzón, Gabriela; Curtidor, Hernando; Vanegas, Magnolia; Vizcaíno, Carolina; Patarroyo, Manuel A.; Patarroyo, Manuel E.

En: Peptides, 01.11.2010, p. 1987-1994.

Resultado de la investigación: Contribución a una revistaArtículo

TY - JOUR

T1 - Conserved high activity binding peptides from the Plasmodium falciparum Pf34 rhoptry protein inhibit merozoites in vitro invasion of red blood cells

AU - Arévalo-Pinzón, Gabriela

AU - Curtidor, Hernando

AU - Vanegas, Magnolia

AU - Vizcaíno, Carolina

AU - Patarroyo, Manuel A.

AU - Patarroyo, Manuel E.

PY - 2010/11/1

Y1 - 2010/11/1

N2 - Rhoptries are specialized secretory organelles found in all members of the genus Plasmodium whose proteins have been considered as promising vaccine candidates due to their involvement in cell invasion and the formation of the parasitophorous vacuole (PV). The Plasmodium falciparum Pf34 protein was recently identified as a rhoptry-neck protein located in detergent-resistant microdomains (DRMs) that is expressed in mature intraerythrocytic parasite stages, but its biological function is still unknown. Receptor-ligand assays carried out in this study found that peptides 36,051 ( 101DKKFSESLKAHMDHLKILNN120Y), 36,053 ( 141KKYIIKEIQNNKYLNKEKKS160), 36,055 ( 181WLESVNNIEEKSNILKNIKS200Y) and 36,056 ( 201QLLNNIASLNHTLSEEIKNI220Y), located in the central portion of Pf34, were found to establish protease-sensitive interactions of high affinity and specificity with receptors on the surface of red blood cell (RBCs). In vitro assays showed that Pf34 high activity binding peptides (HABPs) inhibit invasion of RBCs by P. falciparum merozoites, therefore suggesting that Pf34 could act as an adhesin during invasion and supporting the inclusion of Pf34 HABPs in further studies to develop antimalarial control methods. © 2010 Elsevier Inc. All rights reserved.

AB - Rhoptries are specialized secretory organelles found in all members of the genus Plasmodium whose proteins have been considered as promising vaccine candidates due to their involvement in cell invasion and the formation of the parasitophorous vacuole (PV). The Plasmodium falciparum Pf34 protein was recently identified as a rhoptry-neck protein located in detergent-resistant microdomains (DRMs) that is expressed in mature intraerythrocytic parasite stages, but its biological function is still unknown. Receptor-ligand assays carried out in this study found that peptides 36,051 ( 101DKKFSESLKAHMDHLKILNN120Y), 36,053 ( 141KKYIIKEIQNNKYLNKEKKS160), 36,055 ( 181WLESVNNIEEKSNILKNIKS200Y) and 36,056 ( 201QLLNNIASLNHTLSEEIKNI220Y), located in the central portion of Pf34, were found to establish protease-sensitive interactions of high affinity and specificity with receptors on the surface of red blood cell (RBCs). In vitro assays showed that Pf34 high activity binding peptides (HABPs) inhibit invasion of RBCs by P. falciparum merozoites, therefore suggesting that Pf34 could act as an adhesin during invasion and supporting the inclusion of Pf34 HABPs in further studies to develop antimalarial control methods. © 2010 Elsevier Inc. All rights reserved.

U2 - 10.1016/j.peptides.2010.07.009

DO - 10.1016/j.peptides.2010.07.009

M3 - Article

C2 - 20654670

SP - 1987

EP - 1994

JO - Peptides

JF - Peptides

SN - 0196-9781

ER -