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Vol. 11, Issue 1, 355-368, January 2000
and
*Laboratoire de Biochimie et Biologie Moléculaire des
Insectes, Toxoplasma gondii relies on its actin
cytoskeleton to glide and enter its host cell. However, T.
gondii tachyzoites are known to display a strikingly low amount
of actin filaments, which suggests that sequestration of actin monomers
could play a key role in parasite actin dynamics. We isolated a 27-kDa
tachyzoite protein on the basis of its ability to bind muscle G-actin
and demonstrated that it interacts with parasite G-actin. Cloning and
sequence analysis of the gene coding for this protein, which we named
Toxofilin, showed that it is a novel actin-binding protein. In in vitro
assays, Toxofilin not only bound to G-actin and inhibited actin
polymerization as an actin-sequestering protein but also slowed down
F-actin disassembly through a filament end capping activity. In
addition, when green fluorescent protein-tagged Toxofilin was
overexpressed in mammalian nonmuscle cells, the dynamics of actin
stress fibers was drastically impaired, whereas green fluorescent
protein-Toxofilin copurified with G-actin. Finally, in motile
parasites, during gliding or host cell entry, Toxofilin was localized
in the entire cytoplasm, including the rear end of the parasite,
whereas in intracellular tachyzoites, especially before they exit from
the parasitophorous vacuole of their host cell, Toxofilin was found to
be restricted to the apical end.
Unité de Biologie des Interactions
Cellulaires, Unité de Recherche Associée, Centre National
de la Recherche Scientifique 1960, and Station Centrale
de Microscopie Électronique, Institut Pasteur, 75724 Paris Cedex
15, France
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