@inbook{95625e43a5904dd8ae3490a4a1d078d4,
title = "Receptor affinity-based purification of PfEMP1 proteins",
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 = "Erythrocyte Membrane/metabolism, Erythrocytes/metabolism, Humans, Malaria, Falciparum, Plasmodium falciparum/metabolism, Protozoan Proteins/metabolism",
author = "Olsen, {Rebecca W} and Jennifer Suurbaar and Jensen, {Anja Ramstedt}",
note = "{\textcopyright} 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2022",
doi = "10.1007/978-1-0716-2189-9_22",
language = "English",
volume = "2470",
series = "Methods in molecular biology (Clifton, N.J.)",
publisher = "Humana Press",
pages = "299--308",
booktitle = "Malaria Immunology",
address = "United States",
}