Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • NEWS AND VIEWS

Spotlight on proteins that aid malaria

The multiprotein complex PTEX enables malaria-causing parasites to survive inside red blood cells. Studies reveal how PTEX assembles, and identify a function for one of the complex’s proteins, EXP2.
  1. Tania F. de Koning-Ward

    1. Tania F. de Koning-Ward is in the School of Medicine, Deakin University, Geelong, Victoria 3216, Australia.

    View author publications

    You can also search for this author in PubMed  Google Scholar

Malaria is caused by the parasite Plasmodium falciparum. For part of its life cycle, this organism resides inside human red blood cells in a membrane-bound compartment called a vacuole. To survive, multiply and evade an immune response in this environment, P. falciparum must transport nutrients and proteins across the vacuolar membrane1. Writing in Nature, Ho et al.2 report the structure of the parasite PTEX complex, which resides on the vacuolar membrane and facilitates the export of proteins from the vacuole to the cytoplasm of red blood cells3. And in a paper in Nature Microbiology, Garten et al.4 reveal that the protein EXP2, which forms part of the PTEX protein-conducting channel located in the vacuolar membrane, can also form a channel that facilitates nutrient transfer across the membrane. These insights into the structure and function of key proteins that aid the survival of P. falciparum might help efforts to develop new antimalarial drugs.

Access options

Rent or buy this article

Get just this article for as long as you need it

$39.95

Learn more

Prices may be subject to local taxes which are calculated during checkout

Nature 561, 41-43 (2018)

doi: https://doi.org/10.1038/d41586-018-05977-2

References

  1. de Koning-Ward, T. F. et al. Nature Rev. Microbiol. 4, 494–507 (2016).

    Article  Google Scholar 

  2. Ho, C.-M. et al. Nature 561, 70–75 (2018).

    Article  Google Scholar 

  3. de Koning-Ward, T. F. et al. Nature 459, 945–949 (2009).

    Article  PubMed  Google Scholar 

  4. Garten, M. et al. Nature Microbiol. http://doi.org/10.1038/s41564-018-0222-7 (2018).

    Article  Google Scholar 

  5. Bullen, H. E. et al. J. Biol. Chem. 287, 7871–7884 (2012).

    Article  PubMed  Google Scholar 

  6. Johnson, D. et al. Parasitology 109, 1–9 (1994).

    Article  PubMed  Google Scholar 

  7. Elsworth, B. et al. Nature 511, 587–591 (2014).

    Article  PubMed  Google Scholar 

  8. Beck, J. R., Muralidharan, V., Oksman, A. & Goldberg, D. E. Nature 511, 592–595 (2014).

    Article  PubMed  Google Scholar 

  9. Hakamada, K., Eatanabe, H., Kawano, R., Noguchi, K. & Yohda, M. Biochem. Biophys. Res. Commun. 482, 700–705 (2017).

    Article  PubMed  Google Scholar 

  10. Desai, S. A., Krogstad, D. J. & McCleskey, E. W. Nature 362, 643–646 (1993).

    Article  PubMed  Google Scholar 

  11. Matthews, K. et al. Mol. Microbiol. 89, 1167–1186 (2013).

    Article  PubMed  Google Scholar 

  12. Matz, J. M., Matuschewski, K. & Kooij, T. W. A. Mol. Biochem. Parasitol. 191, 44–52 (2013).

    Article  PubMed  Google Scholar 

Download references

Subjects

Latest on:

Nature Careers

Jobs

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing

Search

Advanced search

Quick links