Abstract：
:A major part of virulence for Plasmodium falciparum malaria infection, the most lethal parasitic disease of humans, results from increased rigidity and adhesiveness of infected host red cells. These changes are caused by parasite proteins exported to the erythrocyte using novel trafficking machinery assembled in the host cell. To understand these unique modifications, we used a large-scale gene knockout strategy combined with functional screens to identify proteins exported into parasite-infected erythrocytes and involved in remodeling these cells. Eight genes were identified encoding proteins required for export of the parasite adhesin PfEMP1 and assembly of knobs that function as physical platforms to anchor the adhesin. Additionally, we show that multiple proteins play a role in generating increased rigidity of infected erythrocytes. Collectively these proteins function as a pathogen secretion system, similar to bacteria and may provide targets for antivirulence based therapies to a disease responsible for millions of deaths annually.
journal_name
Celljournal_title
Cellauthors
Maier AG,Rug M,O'Neill MT,Brown M,Chakravorty S,Szestak T,Chesson J,Wu Y,Hughes K,Coppel RL,Newbold C,Beeson JG,Craig A,Crabb BS,Cowman AFdoi
10.1016/j.cell.2008.04.051subject
Has Abstractpub_date
2008-07-11 00:00:00pages
48-61issue
1eissn
0092-8674issn
1097-4172pii
S0092-8674(08)00691-0journal_volume
134pub_type
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