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Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts

Author

Listed:
  • Sash Lopaticki

    (The Walter and Eliza Hall Institute of Medical Research)

  • Annie S. P. Yang

    (The Walter and Eliza Hall Institute of Medical Research
    University of Melbourne
    Department of Medical Microbiology)

  • Alan John

    (The Walter and Eliza Hall Institute of Medical Research
    University of Melbourne)

  • Nichollas E. Scott

    (University of Melbourne at the Peter Doherty Institute for Infection and Immunity)

  • James P. Lingford

    (The Walter and Eliza Hall Institute of Medical Research)

  • Matthew T. O’Neill

    (The Walter and Eliza Hall Institute of Medical Research)

  • Sara M. Erickson

    (The Walter and Eliza Hall Institute of Medical Research
    University of Melbourne)

  • Nicole C. McKenzie

    (The Walter and Eliza Hall Institute of Medical Research
    University of Melbourne)

  • Charlie Jennison

    (The Walter and Eliza Hall Institute of Medical Research
    University of Melbourne)

  • Lachlan W. Whitehead

    (The Walter and Eliza Hall Institute of Medical Research
    University of Melbourne)

  • Donna N. Douglas

    (University of Alberta)

  • Norman M. Kneteman

    (University of Alberta)

  • Ethan D. Goddard-Borger

    (The Walter and Eliza Hall Institute of Medical Research
    University of Melbourne)

  • Justin A. Boddey

    (The Walter and Eliza Hall Institute of Medical Research
    University of Melbourne)

Abstract

O-glycosylation of the Plasmodium sporozoite surface proteins CSP and TRAP was recently identified, but the role of this modification in the parasite life cycle and its relevance to vaccine design remain unclear. Here, we identify the Plasmodium protein O-fucosyltransferase (POFUT2) responsible for O-glycosylating CSP and TRAP. Genetic disruption of POFUT2 in Plasmodium falciparum results in ookinetes that are attenuated for colonizing the mosquito midgut, an essential step in malaria transmission. Some POFUT2-deficient parasites mature into salivary gland sporozoites although they are impaired for gliding motility, cell traversal, hepatocyte invasion, and production of exoerythrocytic forms in humanized chimeric liver mice. These defects can be attributed to destabilization and incorrect trafficking of proteins bearing thrombospondin repeats (TSRs). Therefore, POFUT2 plays a similar role in malaria parasites to that in metazoans: it ensures the trafficking of Plasmodium TSR proteins as part of a non-canonical glycosylation-dependent endoplasmic reticulum protein quality control mechanism.

Suggested Citation

  • Sash Lopaticki & Annie S. P. Yang & Alan John & Nichollas E. Scott & James P. Lingford & Matthew T. O’Neill & Sara M. Erickson & Nicole C. McKenzie & Charlie Jennison & Lachlan W. Whitehead & Donna N., 2017. "Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts," Nature Communications, Nature, vol. 8(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00571-y
    DOI: 10.1038/s41467-017-00571-y
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    Cited by:

    1. Sash Lopaticki & Robyn McConville & Alan John & Niall Geoghegan & Shihab Deen Mohamed & Lisa Verzier & Ryan W. J. Steel & Cindy Evelyn & Matthew T. O’Neill & Niccolay Madiedo Soler & Nichollas E. Scot, 2022. "Tryptophan C-mannosylation is critical for Plasmodium falciparum transmission," Nature Communications, Nature, vol. 13(1), pages 1-18, December.

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