Identifying Plasmodium falciparum merozoite surface protein-10 human erythrocyte specific binding regions

Alvaro Puentes, Marisol Ocampo, Luis Eduardo Rodríguez, Ricardo Vera, John Valbuena, Hernando Curtidor, Javier García, Ramsés López, Diana Tovar, Jimena Cortes, Zuly Rivera, Manuel Elkin Patarroyo

    Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

    19 Citas (Scopus)

    Resumen

    Receptor-ligand interactions between synthetic peptides and normal human erythrocytes were studied to determine P. falciparum merozoite surface protein-10 (MSP-10) regions specifically binding to membrane surface receptors on human erythrocytes. Three MSP-10 protein High Activity Binding Peptides (HABPs) were identified, whose binding to erythrocytes became saturable and sensitive on being treated with neuraminidase, trypsin and chymotrypsin. Some of them specifically recognised a 50 kDa erythrocyte membrane protein. Some HABPs inhibited in vitro P. falciparum merozoite invasion of erythrocytes by 70%, suggesting that MSP-10 protein's possible role in the invasion process probably functions by using similar mechanisms to those described for other MSP family antigens. In addition to above results, the high homology in amino-acid sequence and superimposition of both MSP-10, MSP-8 and MSP-1 EGF-like domains and HABPs 31132, 26373 and 5501 suggest that tridimensional structure could be playing an important role in the invasion process and in designing synthetic multi-stage anti-malarial vaccines.

    Idioma originalInglés estadounidense
    Páginas (desde-hasta)461-72
    Número de páginas12
    PublicaciónBiochimie
    Volumen87
    N.º5
    DOI
    EstadoPublicada - may 2005

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