Isolation and identification of actin-binding proteins in Plasmodium falciparum by affinity chromatography
Mem. Inst. Oswaldo Cruz
;
95(3): 329-37, May-Jun. 2000. ilus
Artigo
em Inglês
| LILACS
| ID: lil-258186
ABSTRACT
The invasion of the erythrocyte by Plasmodium falciparum depends on the ability of the merozoite to move through the membrane invagination. This ability is probably mediated by actin dependent motors. Using affinity columns with G-actin and F-actin we isolated actin binding proteins from the parasite. By immunoblotting and immunoprecipitation with specific antibodies we identified the presence of tropomyosin, myosin, a-actinin, and two different actins in the eluate corresponding to F-actin binding proteins. In addition to these, a 240-260 kDa doublet, different in size from the erythrocyte spectrin, reacted with an antibody against human spectrin. All the above mentioned proteins were metabolically radiolabeled when the parasite was cultured with 35S-methionine. The presence of these proteins in P. falciparum is indicative of a complex cytoskeleton and supports the proposed role for an actin-myosin motor during invasion.
Texto completo:
DisponíveL
Índice:
LILACS (Américas)
Assunto principal:
Plasmodium falciparum
/
Proteínas dos Microfilamentos
Tipo de estudo:
Estudo diagnóstico
Limite:
Animais
Idioma:
Inglês
Revista:
Mem. Inst. Oswaldo Cruz
Assunto da revista:
Medicina Tropical
/
Parasitologia
Ano de publicação:
2000
Tipo de documento:
Artigo
País de afiliação:
Colômbia
Similares
MEDLINE
...
LILACS
LIS