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

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Listed:
  • Josh R. Beck

    (Washington University School of Medicine)

  • Vasant Muralidharan

    (Washington University School of Medicine
    Howard Hughes Medical Institute, Washington University School of Medicine
    Present address: Center for Tropical and Emerging Global Diseases and Department of Cellular Biology, University of Georgia, Athens, Georgia 30602, USA.)

  • Anna Oksman

    (Washington University School of Medicine
    Washington University School of Medicine
    Howard Hughes Medical Institute, Washington University School of Medicine)

  • Daniel E. Goldberg

    (Washington University School of Medicine
    Washington University School of Medicine
    Howard Hughes Medical Institute, Washington University School of Medicine)

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.

Suggested Citation

  • Josh R. Beck & Vasant Muralidharan & Anna Oksman & Daniel E. Goldberg, 2014. "PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes," Nature, Nature, vol. 511(7511), pages 592-595, July.
    • Handle: RePEc:nat:nature:v:511:y:2014:i:7511:d:10.1038_nature13574
    DOI: 10.1038/nature13574
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