Isolation and identification of actin-binding proteins in Plasmodium falciparum by affinity chromatography.

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.

journal_name

Mem Inst Oswaldo Cruz

authors

Forero C,Wasserman M

doi

10.1590/s0074-02762000000300007

subject

Has Abstract

pub_date

2000-05-01 00:00:00

pages

329-37

issue

3

eissn

0074-0276

issn

1678-8060

pii

S0074-02762000000300007

journal_volume

95

pub_type

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