Specific erythrocyte binding capacity and biological activity of Plasmodium falciparum erythrocyte binding ligand 1 (EBL-1)-derived peptides
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-KIKEMKWICTDNQF...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2005
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/26987
- Acceso en línea:
- https://doi.org/10.1110/ps.041084305
https://repository.urosario.edu.co/handle/10336/26987
- Palabra clave:
- Malaria protein
Erythrocyte binding ligand-1
Peptides
Plasmodium falciparum
- Rights
- License
- Abierto (Texto Completo)
| Summary: | 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. |
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