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
Article
in En
| LILACS
| ID: lil-258186
Responsible library:
BR1.1
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.
Full text:
1
Index:
LILACS
Main subject:
Plasmodium falciparum
/
Microfilament Proteins
Type of study:
Diagnostic_studies
Limits:
Animals
Language:
En
Journal:
Mem. Inst. Oswaldo Cruz
Journal subject:
MEDICINA TROPICAL
/
PARASITOLOGIA
Year:
2000
Type:
Article