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

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

doi:https://doi.org/10.1110/ps.041084305

Ítem

Solo Metadatos

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

https://repository.urosario.edu.co/handle/10336/26987
https://doi.org/10.1110/ps.041084305

Autores

Curtidor, Hernando

Rodríguez, Luis E

Ocampo, Marisol

López, Ramses

García, Javier E

Valbuena, John

Vera, Ricardo

Puentes, Alvaro

Vanegas, Magnolia

Patarroyo, Manuel E

Fecha

2005-02

Editor

The Protein Society
John Wiley & Son

Buscar en:

Métricas alternativas

Abstract

Erythrocyte binding ligand 1 (EBL-1) is a member of the ebl multigene family involved in Plasmodiumfalciparum 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 wassaturable, not sialic acid-dependent, and that all peptides specifically bound to a 36-kDa protein on theerythrocyte membrane. The five HABPs inhibited in vitro merozoite invasion depending on the peptideconcentration used, suggesting their possible role in the invasion process.