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. 2022:2470:299-308.
doi: 10.1007/978-1-0716-2189-9_22.

Receptor Affinity-Based Purification of PfEMP1 Proteins

Rebecca W Olsen  1 , Jennifer Suurbaar  2   3 , Anja Ramstedt Jensen  4
Affiliations

Receptor Affinity-Based Purification of PfEMP1 Proteins

Rebecca W Olsen et al. Methods Mol Biol. 2022.

Abstract

The virulence of Plasmodium falciparum is linked to the ability of infected erythrocytes (IEs) to bind a range of human receptors. This binding is mediated by a family of highly polymorphic proteins known as P. falciparum erythrocyte membrane protein 1 (PfEMP1). PfEMP1 proteins are expressed on the surface of IEs and are composed of extracellular domains (NTS, CIDR, DBL), a transmembrane region and an acidic C-terminal segment. Subdomains of the extracellular N-terminal part of PfEMP1 molecules have been shown to bind specific receptors.In this chapter, we describe how to purify PfEMP1 proteins by a receptor affinity-based method. This includes how to prepare affinity columns and how to subsequently test the functionality of the purified PfEMP1 protein in an ELISA-based assay.

Keywords: Affinity purification; CIDR; DBL; ELISA; Ligand–receptor interaction; Malaria; PfEMP1.

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References

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