Receptor–ligand and parasite protein–protein interactions in Plasmodium vivax: Analysing rhoptry neck proteins 2 and 4

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

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

12 Citas (Scopus)


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 receptGuardarors 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.

Idioma originalInglés estadounidense
Número de artículoe12835
PublicaciónCellular Microbiology
EstadoPublicada - jul. 2018

Áreas temáticas de ASJC Scopus

  • Microbiología
  • Inmunología
  • Virología


Profundice en los temas de investigación de 'Receptor–ligand and parasite protein–protein interactions in Plasmodium vivax: Analysing rhoptry neck proteins 2 and 4'. En conjunto forman una huella única.

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