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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/21098


Title: Isolation and Identification of Actin-binding Proteins in Plasmodium falciparum by Affinity Chromatography
Authors: Forero, Claudia
Wasserman, Moiss
Keywords: actin, a-actinin, malaria, myosin, spectrin, tropomyosin, Plasmodium falciparum, affinity chromatography
Issue Date: 31-Dec-2000
Publisher: Fundação Oswaldo Cruz, Fiocruz
Citation: Memórias do Instituto Oswaldo Cruz (ISSN: 1678-8060) Vol 95 Num 3
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.
URI: http://hdl.handle.net/1807/21098
Other Identifiers: http://www.bioline.org.br/abstract?id=oc00055
Rights: Copyright 2000 Fundacao Oswaldo Cruz Fiocruz
Appears in Collections:Bioline International Legacy Collection

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