The structural basis for CD36 binding by the malaria parasite

Research output: Contribution to journal › Journal article › Research › peer-review

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The structural basis for CD36 binding by the malaria parasite. / Hsieh, Fu-Lien; Turner, Louise; Bolla, Jani Reddy; Robinson, Carol V; Lavstsen, Thomas; Higgins, Matthew K.

In: Nature Communications, Vol. 7, 12837, 27.09.2016.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hsieh, F-L, Turner, L, Bolla, JR, Robinson, CV, Lavstsen, T & Higgins, MK 2016, 'The structural basis for CD36 binding by the malaria parasite', Nature Communications, vol. 7, 12837. https://doi.org/10.1038/ncomms12837

APA

Hsieh, F-L., Turner, L., Bolla, J. R., Robinson, C. V., Lavstsen, T., & Higgins, M. K. (2016). The structural basis for CD36 binding by the malaria parasite. Nature Communications, 7, [12837]. https://doi.org/10.1038/ncomms12837

Vancouver

Hsieh F-L, Turner L, Bolla JR, Robinson CV, Lavstsen T, Higgins MK. The structural basis for CD36 binding by the malaria parasite. Nature Communications. 2016 Sep 27;7. 12837. https://doi.org/10.1038/ncomms12837

Author

Hsieh, Fu-Lien ; Turner, Louise ; Bolla, Jani Reddy ; Robinson, Carol V ; Lavstsen, Thomas ; Higgins, Matthew K. / The structural basis for CD36 binding by the malaria parasite. In: Nature Communications. 2016 ; Vol. 7.

Bibtex

@article{d8ff633a6a9b4a3686028a21f361b8be,
title = "The structural basis for CD36 binding by the malaria parasite",
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.",
author = "Fu-Lien Hsieh and Louise Turner and Bolla, {Jani Reddy} and Robinson, {Carol V} and Thomas Lavstsen and Higgins, {Matthew K}",
year = "2016",
month = sep,
day = "27",
doi = "10.1038/ncomms12837",
language = "English",
volume = "7",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - The structural basis for CD36 binding by the malaria parasite

AU - Hsieh, Fu-Lien

AU - Turner, Louise

AU - Bolla, Jani Reddy

AU - Robinson, Carol V

AU - Lavstsen, Thomas

AU - Higgins, Matthew K

PY - 2016/9/27

Y1 - 2016/9/27

N2 - 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.

AB - 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.

U2 - 10.1038/ncomms12837

DO - 10.1038/ncomms12837

M3 - Journal article

C2 - 27667267

VL - 7

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 12837

ER -

ID: 166379829