Related Experiment Video
Updated: Sep 3, 2025

Author Spotlight: Optimizing Affinity Chromatography for His-Tagged FEN1 Protein
Published on: April 26, 2024
Receptor Affinity-Based Purification of PfEMP1 Proteins
Rebecca W Olsen1, Jennifer Suurbaar2,3, Anja Ramstedt Jensen4
1Department of Immunology and Microbiology, Faculty of Health and Medical Sciences, Centre for Medical Parasitology, University of Copenhagen, Copenhagen, Denmark. rwo@gubra.dk.
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.
Related Concept Videos
Immunoprecipitation
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
Tagging and Fusion Proteins

