| Literature DB >> 15659376 |
Hernando Curtidor1, Luis E Rodríguez, Marisol Ocampo, Ramses López, Javier E García, John Valbuena, Ricardo Vera, Alvaro Puentes, Magnolia Vanegas, Manuel E Patarroyo.
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.Entities:
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Year: 2005 PMID: 15659376 PMCID: PMC2254251 DOI: 10.1110/ps.041084305
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725