PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes

Josh R. Beck, Vasant Muralidharan, Anna Oksman and Daniel E. Goldberg ()
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Josh R. Beck: Washington University School of Medicine
Vasant Muralidharan: Washington University School of Medicine
Anna Oksman: Washington University School of Medicine
Daniel E. Goldberg: Washington University School of Medicine

Nature, 2014, vol. 511, issue 7511, 592-595

Abstract: Plasmodium parasites, the causative agent of malaria, infect and remodel red blood cells by exporting hundreds of proteins into the red blood cell cytosol, a topological conundrum given that the parasite resides in a compartment known as the parasitophorous vacuole; here a dihydrofolate-reductase-based destabilization domain approach is used to inactivate HSP101, part of the Plasmodium translocon of exported proteins, and to demonstrate that it is required for the secretion of all classes of exported Plasmodium proteins.

Date: 2014
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DOI: 10.1038/nature13574

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