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Updated: Sep 3, 2025
High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension
Published on: December 28, 2015
Expression of Large Full-Length PfEMP1 Proteins in HEK293 Cells
Jonathan Paul Renn1, Justin Yai Alamou Doritchamou1, Patrick Emmet Duffy2
1Laboratory of Malaria Immunology and Vaccinology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
None:
Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is a family of proteins expressed on the surface of red blood cells infected by Plasmodium falciparum. PfEMP1 proteins play a vital role in parasite virulence, and thus are important vaccine candidates to prevent severe disease. VAR2CSA is one specific PfEMP1 essential for pregnancy malaria pathogenesis, and the primary target in pregnancy malaria vaccine development. However, similar to other PfEMP1 proteins, expression of recombinant full-length VAR2CSA is difficult due to its large size, multidomain architecture and high cysteine content. To date, there has been success using higher ordered expression systems (such as mammalian and insect cells) to generate folded and active VAR2CSA. However, recent improvements with mammalian expression systems including cell lines and promoters have pushed the boundaries of yields. Here, we describe a modified protocol beyond current systems that enhances yields of full-length VAR2CSA and can generate higher quantities of material for protein structural and functional characterization.
