A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion

Malaria parasites invade host cells using actin-based motility, a process requiring parasite actin filament nucleation and polymerization. Malaria and other apicomplexan parasites lack Arp2/3 complex, an actin nucleator widely conserved across eukaryotes, but do express formins, another type of acti...

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Bibliographic Details
Published in:Cell host & microbe 2008-03, Vol.3 (3), p.188-198
Main Authors: Baum, Jake, Tonkin, Christopher J, Paul, Aditya S, Rug, Melanie, Smith, Brian J, Gould, Sven B, Richard, Dave, Pollard, Thomas D, Cowman, Alan F
Format: Article
Language:English
Subjects:
Actins - metabolism
Animals
Cell Line
Cercopithecus aethiops
Cytosol - chemistry
Erythrocytes - chemistry
Erythrocytes - parasitology
Fetal Proteins - metabolism
Humans
Microfilament Proteins - metabolism
Microscopy, Fluorescence
Models, Molecular
Nuclear Proteins - metabolism
Plasmodium falciparum
Plasmodium falciparum - physiology
Protein Binding
Protozoan Proteins - metabolism
Tight Junctions - chemistry
Toxoplasma - physiology
Toxoplasma gondii
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Summary:Malaria parasites invade host cells using actin-based motility, a process requiring parasite actin filament nucleation and polymerization. Malaria and other apicomplexan parasites lack Arp2/3 complex, an actin nucleator widely conserved across eukaryotes, but do express formins, another type of actin nucleator. Here, we demonstrate that one of two malaria parasite formins, Plasmodium falciparum formin 1 (PfFormin 1), and its ortholog in the related parasite Toxoplasma gondii, follows the moving tight junction between the invading parasite and the host cell, which is the predicted site of the actomyosin motor that powers motility. Furthermore, in vitro, the PfFormin1 actin-binding formin homology 2 domain is a potent nucleator, stimulating actin polymerization and, like other formins, localizing to the barbed end during filament elongation. These findings support a conserved molecular mechanism underlying apicomplexan parasite motility and, given the essential role that actin plays in cell invasion, highlight formins as important determinants of malaria parasite pathogenicity.
ISSN:1931-3128
1934-6069
DOI:10.1016/j.chom.2008.02.006