Receptor affinity-based purification of PfEMP1 proteins

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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 languageEnglish
Title of host publicationMalaria Immunology : Targeting the Surface of Infected Erythrocytes
Number of pages10
Volume2470
PublisherHumana Press
Publication date2022
Pages299-308
ISBN (Electronic)978-1-0716-2189-9
DOIs
Publication statusPublished - 2022
SeriesMethods in molecular biology (Clifton, N.J.)
ISSN1064-3745

Bibliographical note

© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

    Research areas

  • Erythrocyte Membrane/metabolism, Erythrocytes/metabolism, Humans, Malaria, Falciparum, Plasmodium falciparum/metabolism, Protozoan Proteins/metabolism

ID: 320648912