Receptor-ligand and parasite protein-protein interactions in Plasmodium vivax

Analysing rhoptry neck proteins 2 and 4

Título traducido de la contribución: Interacciones entre proteínas receptoras y parásitas en Plasmodium vivax: Análisis de las proteínas 2 y 4 del cuello de la róptria

Gabriela Arévalo-Pinzón, Laura Rubio, Olivier Chaloin, Sylviane Muller, Hernando Curtidor, Manuel Alfonso Patarroyo, Maritza Bermúdez

Resultado de la investigación: Contribución a RevistaArtículo

3 Citas (Scopus)

Resumen

Las interacciones receptor-ligando y proteína-proteína representan una alternativa atractiva para el diseño de métodos efectivos de control de Plasmodium vivax. Este artículo describe la capacidad de las proteínas 2 y 4 (RON2 y RON4) de P. vivax para unirse a los reticulocitos humanos. Estudios bioquímicos y celulares han demostrado que dos regiones conservadas derivadas de PvRON2 y PvRON4 interactúan específicamente con receptores de proteínas en reticulocitos marcados por el receptor de transferrina de superficie CD71. El mapeo de la región de unión de cada fragmento de proteína llevó a definir la participación específica de dos regiones de 20 aminoácidos de longitud que compiten selectivamente por PvRON2 y PvRON4 que se unen a los reticulocitos. Las interacciones binarias entre el PvRON2 (ligando) y otras proteínas del parásito, como el PvRON4, el PvRON5 y el antígeno de la membrana apical 1 (AMA1), fueron evaluadas y caracterizadas por la resonancia plasmónica superficial. Los resultados revelaron que ambas regiones ricas en cisteína del PvRON2 interactúan fuertemente con los dominios II y III del PvAMA1 (constantes de equilibrio en el rango nanomolar) y en menor medida con el ectodominio completo del PvAMA1 y los dominios I y II. Estos resultados apoyan firmemente que estas proteínas participan en el complejo proceso de invasión de P. vivax, proporcionando así nuevas dianas pertinentes para bloquear la entrada específica de los merozoitos de P. vivax a sus células diana.
Idioma originalEnglish (US)
Páginas (desde-hasta)e12835
PublicaciónCellular Microbiology
Volumen20
N.º7
DOI
EstadoPublished - feb 27 2018
Publicado de forma externa

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Arévalo-Pinzón, Gabriela ; Rubio, Laura ; Chaloin, Olivier ; Muller, Sylviane ; Curtidor, Hernando ; Patarroyo, Manuel Alfonso ; Bermúdez, Maritza. / Receptor-ligand and parasite protein-protein interactions in Plasmodium vivax : Analysing rhoptry neck proteins 2 and 4. En: Cellular Microbiology. 2018 ; Vol. 20, N.º 7. pp. e12835.
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title = "Receptor-ligand and parasite protein-protein interactions in Plasmodium vivax: Analysing rhoptry neck proteins 2 and 4",
abstract = "Elucidating receptor-ligand and protein-protein interactions represents an attractive alternative for designing effective Plasmodium vivax control methods. This article describes the ability of P. vivax rhoptry neck proteins 2 and 4 (RON2 and RON4) to bind to human reticulocytes. Biochemical and cellular studies have shown that two PvRON2- and PvRON4-derived conserved regions specifically interact with protein receptors on reticulocytes marked by the CD71 surface transferrin receptor. Mapping each protein fragment's binding region led to defining the specific participation of two 20 amino acid-long regions selectively competing for PvRON2 and PvRON4 binding to reticulocytes. Binary interactions between PvRON2 (ligand) and other parasite proteins, such as PvRON4, PvRON5, and apical membrane antigen 1 (AMA1), were evaluated and characterised by surface plasmon resonance. The results revealed that both PvRON2 cysteine-rich regions strongly interact with PvAMA1 Domains II and III (equilibrium constants in the nanomolar range) and at a lower extent with the complete PvAMA1 ectodomain and Domains I and II. These results strongly support that these proteins participate in P. vivax's complex invasion process, thus providing new pertinent targets for blocking P. vivax merozoites' specific entry to their target cells.",
author = "Gabriela Ar{\'e}valo-Pinz{\'o}n and Laura Rubio and Olivier Chaloin and Sylviane Muller and Hernando Curtidor and Patarroyo, {Manuel Alfonso} and Maritza Berm{\'u}dez",
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Receptor-ligand and parasite protein-protein interactions in Plasmodium vivax : Analysing rhoptry neck proteins 2 and 4. / Arévalo-Pinzón, Gabriela; Rubio, Laura; Chaloin, Olivier; Muller, Sylviane; Curtidor, Hernando; Patarroyo, Manuel Alfonso; Bermúdez, Maritza.

En: Cellular Microbiology, Vol. 20, N.º 7, 27.02.2018, p. e12835.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Receptor-ligand and parasite protein-protein interactions in Plasmodium vivax

T2 - Analysing rhoptry neck proteins 2 and 4

AU - Arévalo-Pinzón, Gabriela

AU - Rubio, Laura

AU - Chaloin, Olivier

AU - Muller, Sylviane

AU - Curtidor, Hernando

AU - Patarroyo, Manuel Alfonso

AU - Bermúdez, Maritza

N1 - © 2018 John Wiley & Sons Ltd.

PY - 2018/2/27

Y1 - 2018/2/27

N2 - Elucidating receptor-ligand and protein-protein interactions represents an attractive alternative for designing effective Plasmodium vivax control methods. This article describes the ability of P. vivax rhoptry neck proteins 2 and 4 (RON2 and RON4) to bind to human reticulocytes. Biochemical and cellular studies have shown that two PvRON2- and PvRON4-derived conserved regions specifically interact with protein receptors on reticulocytes marked by the CD71 surface transferrin receptor. Mapping each protein fragment's binding region led to defining the specific participation of two 20 amino acid-long regions selectively competing for PvRON2 and PvRON4 binding to reticulocytes. Binary interactions between PvRON2 (ligand) and other parasite proteins, such as PvRON4, PvRON5, and apical membrane antigen 1 (AMA1), were evaluated and characterised by surface plasmon resonance. The results revealed that both PvRON2 cysteine-rich regions strongly interact with PvAMA1 Domains II and III (equilibrium constants in the nanomolar range) and at a lower extent with the complete PvAMA1 ectodomain and Domains I and II. These results strongly support that these proteins participate in P. vivax's complex invasion process, thus providing new pertinent targets for blocking P. vivax merozoites' specific entry to their target cells.

AB - Elucidating receptor-ligand and protein-protein interactions represents an attractive alternative for designing effective Plasmodium vivax control methods. This article describes the ability of P. vivax rhoptry neck proteins 2 and 4 (RON2 and RON4) to bind to human reticulocytes. Biochemical and cellular studies have shown that two PvRON2- and PvRON4-derived conserved regions specifically interact with protein receptors on reticulocytes marked by the CD71 surface transferrin receptor. Mapping each protein fragment's binding region led to defining the specific participation of two 20 amino acid-long regions selectively competing for PvRON2 and PvRON4 binding to reticulocytes. Binary interactions between PvRON2 (ligand) and other parasite proteins, such as PvRON4, PvRON5, and apical membrane antigen 1 (AMA1), were evaluated and characterised by surface plasmon resonance. The results revealed that both PvRON2 cysteine-rich regions strongly interact with PvAMA1 Domains II and III (equilibrium constants in the nanomolar range) and at a lower extent with the complete PvAMA1 ectodomain and Domains I and II. These results strongly support that these proteins participate in P. vivax's complex invasion process, thus providing new pertinent targets for blocking P. vivax merozoites' specific entry to their target cells.

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