ArticleJournal of visualized experiments : JoVE2015
HeLa Based Cell Free Expression Systems for Expression of Plasmodium Rhoptry Proteins.
Article in Journal of visualized experiments : JoVE, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Eukaryotic cell-free protein synthesis: Chassis diversification, system engineering, and emerging applications.Synthetic and systems biotechnology · 2026Review
- Article
- Cell-Free Protein Synthesis: A Promising Option for Future Drug Development.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2020Review
- Design, Development and Optimization of a Functional Mammalian Cell-Free Protein Synthesis Platform.Frontiers in bioengineering and biotechnology · 2020Article
- Accelerating the Production of Druggable Targets: Eukaryotic Cell-Free Systems Come into Focus.Methods and protocols · 2019Article
- A User's Guide to Cell-Free Protein Synthesis.Methods and protocols · 2019Review
- Self-assembling functional programmable protein array for studying protein-protein interactions in malaria parasites.Malaria journal · 2018Article
- Non-conventional expression systems for the production of vaccine proteins and immunotherapeutic molecules.Human vaccines & immunotherapeutics · 2017Review
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Malaria causes significant global morbidity and mortality. No routine vaccine is currently available. One of the major reasons for lack of a vaccine is the challenge of identifying suitable vaccine candidates. Malarial proteins expressed using prokaryotic and eukaryotic cell based expression systems are poorly glycosylated, generally insoluble and undergo improper folding leading to reduced immunogenicity. The wheat germ, rabbit reticulocyte lysate and Escherichia coli lysate cell free expression systems are currently used for expression of malarial proteins. However, the length of expression time and improper glycosylation of proteins still remains a challenge. We demonstrate expression of Plasmodium proteins in vitro using HeLa based cell free expression systems, termed "in vitro human cell free expression systems". The 2 HeLa based cell free expression systems transcribe mRNA in 75 min and 3 µl of transcribed mRNA is sufficient to translate proteins in 90 min. The 1-step expression system is a transcription and translation coupled expression system; the transcription and co-translation occurs in 3 hr. The process can also be extended for 6 hr by providing additional energy. In the 2-step expression system, mRNA is first transcribed and then added to the translation mix for protein expression. We describe how to express malaria proteins; a hydrophobic PF3D7_0114100 Maurer's Cleft - 2 transmembrane (PfMC-2TM) protein, a hydrophilic PF3D7_0925900 protein and an armadillo repeats containing protein PF3D7_1361800, using the HeLa based cell free expression system. The proteins are expressed in micro volumes employing 2-step and 1-step expression strategies. An affinity purification method to purify 25 µl of proteins expressed using the in vitro human cell free expression system is also described. Protein yield is determined by Bradford's assay and the expressed and purified proteins can be confirmed by western blotting analysis. Expressed recombinant proteins can be used for immunizations, immunoassays and protein sequencing.
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