Format

Send to

Choose Destination
See comment in PubMed Commons below
Cell. 2008 Jul 11;134(1):48-61. doi: 10.1016/j.cell.2008.04.051.

Exported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytes.

Author information

1
The Walter and Eliza Hall Institute of Medical Research, Melbourne 3050, Australia.

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.

PMID:
18614010
PMCID:
PMC2568870
DOI:
10.1016/j.cell.2008.04.051
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center