The structural basis for CD36 binding by the malaria parasite

Fu-Lien Hsieh; Louise Turner; Jani Reddy Bolla; Carol V. Robinson; Thomas Lavstsen; Matthew K. Higgins

doi:10.1038/ncomms12837

Nature Communications (Sep 2016)

The structural basis for CD36 binding by the malaria parasite

Fu-Lien Hsieh,
Louise Turner,
Jani Reddy Bolla,
Carol V. Robinson,
Thomas Lavstsen,
Matthew K. Higgins

Affiliations

Fu-Lien Hsieh: Department of Biochemistry, University of Oxford
Louise Turner: Department of International Health, University of Copenhagen and Department of Infectious Diseases, 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: Department of International Health, University of Copenhagen and Department of Infectious Diseases, Centre for Medical Parasitology, Immunology & Microbiology
Matthew K. Higgins: Department of Biochemistry, University of Oxford

DOI: https://doi.org/10.1038/ncomms12837
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 11

Abstract

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Targeting of the CD36 scavenger receptor by the malaria parasite effector PfEMP1 prevents splenic clearance of infected erythrocytes. Here, the authors propose that diverse PfEMP1 achieve this by binding to a conserved phenylalanine residue in CD36 that is also required for lipoprotein binding.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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