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Updated: Feb 3, 2026
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Separation of Plasmodium falciparum Late Stage-infected Erythrocytes by Magnetic Means
Published on: March 2, 2013
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Plasmodium falciparum-CD36 Structure-Function Relationships Defined by Ortholog Scanning Mutagenesis
Ana Cabrera1, Dante Neculai2, Vanessa Tran1
1SAR Laboratories, Sandra Rotman Centre, Toronto General Hospital-University Health Network, Ontario, Canada.
The Journal of Infectious Diseases
|October 19, 2018
Summary
Malaria parasite binding to CD36 receptors requires a charged surface. Subtle changes in CD36 structure influence how it binds to Plasmodium falciparum-infected erythrocytes (IEs).
Area of Science:
- Structural biology
- Parasitology
- Immunology
Background:
- The interaction between Plasmodium falciparum-infected erythrocytes (IEs) and the host receptor CD36 is a critical host-parasite interface.
- CD36, a scavenger receptor, binds to erythrocyte membrane protein 1 (PfEMP1) on IEs, but orthologs show varied IE binding.
- Understanding this interaction is key to combating malaria.
Purpose of the Study:
- To investigate malaria-CD36 structure-function relationships.
- To define the binding interactions between IEs and CD36.
- To leverage differences in CD36 ortholog binding and structural data.
Main Methods:
- Utilized crystal structure and 3D modeling of CD36.
- Exploited differential binding of IEs to CD36 orthologs.
- Investigated structure-function relationships of malaria-CD36 interactions.
Main Results:
- A charged surface in the membrane-distal region of CD36 is essential for IE binding.
- Additional CD36 domains, near and far, influence IE interaction with this binding site.
- Subtle sequence and spatial variations in CD36 domains modulate receptor conformation.
Conclusions:
- CD36 receptor conformation is regulated by subtle sequence and spatial differences.
- These variations control CD36's selective interaction with diverse ligands.
- The study refines our understanding of malaria parasite binding mechanisms.
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