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The structural basis for CD36 binding by the malaria parasite

Author

Listed:
  • Fu-Lien Hsieh

    (University of Oxford)

  • Louise Turner

    (Centre for Medical Parasitology, Immunology & Microbiology)

  • Jani Reddy Bolla

    (Physical and Theoretical Chemistry Laboratory, University of Oxford)

  • Carol V. Robinson

    (Physical and Theoretical Chemistry Laboratory, University of Oxford)

  • Thomas Lavstsen

    (Centre for Medical Parasitology, Immunology & Microbiology)

  • Matthew K. Higgins

    (University of Oxford)

Abstract

CD36 is a scavenger receptor involved in fatty acid metabolism, innate immunity and angiogenesis. It interacts with lipoprotein particles and facilitates uptake of long chain fatty acids. It is also the most common target of the PfEMP1 proteins of the malaria parasite, Plasmodium falciparum, tethering parasite-infected erythrocytes to endothelial receptors. This prevents their destruction by splenic clearance and allows increased parasitaemia. Here we describe the structure of CD36 in complex with long chain fatty acids and a CD36-binding PfEMP1 protein domain. A conserved hydrophobic pocket allows the hugely diverse PfEMP1 protein family to bind to a conserved phenylalanine residue at the membrane distal tip of CD36. This phenylalanine is also required for CD36 to interact with lipoprotein particles. By targeting a site on CD36 that is required for its physiological function, PfEMP1 proteins maintain the ability to tether to the endothelium and avoid splenic clearance.

Suggested Citation

  • Fu-Lien Hsieh & Louise Turner & Jani Reddy Bolla & Carol V. Robinson & Thomas Lavstsen & Matthew K. Higgins, 2016. "The structural basis for CD36 binding by the malaria parasite," Nature Communications, Nature, vol. 7(1), pages 1-11, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12837
    DOI: 10.1038/ncomms12837
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    Cited by:

    1. V. S. Peche & T. A. Pietka & M. Jacome-Sosa & D. Samovski & H. Palacios & G. Chatterjee-Basu & A. C. Dudley & W. Beatty & G. A. Meyer & I. J. Goldberg & N. A. Abumrad, 2023. "Endothelial cell CD36 regulates membrane ceramide formation, exosome fatty acid transfer and circulating fatty acid levels," Nature Communications, Nature, vol. 14(1), pages 1-19, December.

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