Receptor affinity-based purification of PfEMP1 proteins
Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
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.
Original language | English |
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Title of host publication | Malaria Immunology : Targeting the Surface of Infected Erythrocytes |
Number of pages | 10 |
Volume | 2470 |
Publisher | Humana Press |
Publication date | 2022 |
Pages | 299-308 |
ISBN (Electronic) | 978-1-0716-2189-9 |
DOIs | |
Publication status | Published - 2022 |
Series | Methods in molecular biology (Clifton, N.J.) |
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ISSN | 1064-3745 |
Bibliographical note
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
- Erythrocyte Membrane/metabolism, Erythrocytes/metabolism, Humans, Malaria, Falciparum, Plasmodium falciparum/metabolism, Protozoan Proteins/metabolism
Research areas
ID: 320648912