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Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers

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  • Vasant Muralidharan

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

  • Anna Oksman

    (Howard Hughes Medical Institute, Washington University School of Medicine in St. Louis
    Washington University School of Medicine in St. Louis)

  • Priya Pal

    (Howard Hughes Medical Institute, Washington University School of Medicine in St. Louis
    Washington University School of Medicine in St. Louis)

  • Susan Lindquist

    (Howard Hughes Medical Institute, Washington University School of Medicine in St. Louis
    Whitehead Institute for Biomedical Research
    Massachusetts Institute of Technology)

  • Daniel E. Goldberg

    (Howard Hughes Medical Institute, Washington University School of Medicine in St. Louis
    Washington University School of Medicine in St. Louis)

Abstract

One-fourth of Plasmodium falciparum proteins have asparagine repeats that increase the propensity for aggregation, especially at elevated temperatures that occur routinely in malaria-infected patients. Here we report that a Plasmodium Asn repeat-containing protein (PFI1155w) formed aggregates in mammalian cells at febrile temperatures, as did a yeast Asn/Gln-rich protein (Sup35). Co-expression of the cytoplasmic P. falciparum heat shock protein 110 (PfHsp110c) prevented aggregation. Human or yeast orthologs were much less effective. All-Asn and all-Gln versions of Sup35 were protected from aggregation by PfHsp110c, suggesting that this chaperone is not limited to handling runs of asparagine. PfHsp110c gene-knockout parasites were not viable and conditional knockdown parasites died slowly in the absence of protein-stabilizing ligand. When exposed to brief heat shock, these knockdowns were unable to prevent aggregation of PFI1155w or Sup35 and died rapidly. We conclude that PfHsp110c protects the parasite from harmful effects of its asparagine repeat-rich proteome during febrile episodes.

Suggested Citation

  • Vasant Muralidharan & Anna Oksman & Priya Pal & Susan Lindquist & Daniel E. Goldberg, 2012. "Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers," Nature Communications, Nature, vol. 3(1), pages 1-10, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms2306
    DOI: 10.1038/ncomms2306
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    1. Gerry Q Tonkin-Hill & Leily Trianty & Rintis Noviyanti & Hanh H T Nguyen & Boni F Sebayang & Daniel A Lampah & Jutta Marfurt & Simon A Cobbold & Janavi S Rambhatla & Malcolm J McConville & Stephen J R, 2018. "The Plasmodium falciparum transcriptome in severe malaria reveals altered expression of genes involved in important processes including surface antigen–encoding var genes," PLOS Biology, Public Library of Science, vol. 16(3), pages 1-40, March.
    2. Liqing Hu & Cancan Sun & Justin M. Kidd & Jizhong Han & Xianjun Fang & Hongtao Li & Qingdai Liu & Aaron E. May & Qianbin Li & Lei Zhou & Qinglian Liu, 2023. "A first-in-class inhibitor of Hsp110 molecular chaperones of pathogenic fungi," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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