Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum erythrocyte binding ligand 1 (EBL-1)-derived peptides

Hernando Curtidor, Luis E Rodríguez, Marisol Ocampo, Ramses López, Javier E García, John Valbuena, Ricardo Vera, Alvaro Puentes, Magnolia Vanegas, Manuel E Patarroyo

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    11 Scopus citations

    Abstract

    Erythrocyte binding ligand 1 (EBL-1) is a member of the ebl multigene family involved in Plasmodium falciparum invasion of erythrocytes. We found that five EBL-1 high-activity binding peptides (HABPs) bound specifically to erythrocytes: 29895 ((41)HKKKSGELNNNKSGILRSTY(60)), 29903 ((201)LYECGK-KIKEMKWICTDNQF(220)), 29923 ((601)CNAILGSYADIGDIVRGLDV(620)), 29924((621)WRDINTNKLSEK-FQKIFMGGY(640)), and 30018 ((2481)LEDIINLSKKKKKSINDTSFY(2500)). We also show that binding was saturable, not sialic acid-dependent, and that all peptides specifically bound to a 36-kDa protein on the erythrocyte membrane. The five HABPs inhibited in vitro merozoite invasion depending on the peptide concentration used, suggesting their possible role in the invasion process.

    Original languageEnglish (US)
    Pages (from-to)464 - 473
    Number of pages10
    JournalProtein Science
    Volume14
    Issue number2
    DOIs
    StatePublished - Feb 2005

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