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Protein Science (2005), 14:464-473. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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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, Álvaro Puentes, Magnolia Vanegas and Manuel E. Patarroyo

Fundación Instituto de Inmunología de Colombia and Universidad Nacional de Colombia, Bogotá, Colombia

(RECEIVED August 30, 2004; FINAL REVISION October 4, 2004; ACCEPTED October 9, 2004)

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 (41HKKKSGELNNNKSGILRSTY60), 29903 (201LYECGK-KIKEMKWICTDNQF220), 29923 (601CNAILGSYADIGDIVRGLDV620), 29924(621WRDINTNKLSEK-FQKIFMGGY640), and 30018 (2481LEDIINLSKKKKKSINDTSFY2500). 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.

Keywords: malaria protein; erythrocyte binding ligand-1; peptides; Plasmodium falciparum

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041084305.


Reprint requests to: Hernando Curtidor, Fundación Instituto de Inmunología de Colombia, Carrera 50 No. 26-00, Bogotá, Colombia, 020304 Zona CAN; e-mail: hernando_curtidor{at}fidic.org.co; fax: +57-1-3244672/73 x108.


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