Studies of plasmodium falciparum rhoptry-associated membrane antigen (RAMA) protein peptides specifically binding to human RBC
Plasmodium falciparum rhoptry-associated membrane antigen (RAMA) peptides used in normal red blood cell (RBC) binding assays revealed that peptides 33426 (79NINILSSVHRKGRILYDSF97) and 33460 (777HKKREKSISPHSYQKVSTKVQ797) bound with high activity, presenting nanomolar affinity constants. Such high bin...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2008
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/27002
- Acceso en línea:
- https://doi.org/10.1016/j.vaccine.2007.11.086
https://repository.urosario.edu.co/handle/10336/27002
- Palabra clave:
- P. falciparum
RAMA
Rhoptry
HABP
- Rights
- License
- Restringido (Acceso a grupos específicos)
Summary: | Plasmodium falciparum rhoptry-associated membrane antigen (RAMA) peptides used in normal red blood cell (RBC) binding assays revealed that peptides 33426 (79NINILSSVHRKGRILYDSF97) and 33460 (777HKKREKSISPHSYQKVSTKVQ797) bound with high activity, presenting nanomolar affinity constants. Such high binding activity peptides (HABPs) displayed helicoid and random coil structures as determined by circular dichroism. HABPs inhibited P. falciparum in vitro invasion of normal RBC by up to 61% (depending on concentration), suggesting that some RAMA protein regions could be involved in P. falciparum invasion of RBC. The nature and localisation of receptors on RBC surface responsible for HABP binding were studied using enzyme-treated erythrocytes and structural analysis. |
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