Abstract
BackgroundAlthough there are many different expression systems for recombinant production of pharmaceutical proteins, many of these suffer from drawbacks such as yield, cost, complexity of purification, and possible contamination with human pathogens. Microalgae have enormous potential for diverse biotechnological applications and currently attract much attention in the biofuel sector. Still underestimated, though, is the idea of using microalgae as solar-fueled expression system for the production of recombinant proteins.ResultsIn this study, we show for the first time that completely assembled and functional human IgG antibodies can not only be expressed to high levels in algal systems, but also secreted very efficiently into the culture medium. We engineered the diatom Phaeodactylum tricornutum to synthesize and secrete a human IgG antibody against the Hepatitis B Virus surface protein. As the diatom P. tricornutum is not known to naturally secrete many endogenous proteins, the secreted antibodies are already very pure making extensive purification steps redundant and production extremely cost efficient.ConclusionsMicroalgae combine rapid growth rates with all the advantages of eukaryotic expression systems, and offer great potential for solar-powered, low cost production of pharmaceutical proteins.
Highlights
There are many different expression systems for recombinant production of pharmaceutical proteins, many of these suffer from drawbacks such as yield, cost, complexity of purification, and possible contamination with human pathogens
We show for the first time that a microalgal system like the diatom P. tricornutum is able to secrete a fully assembled and functional human Immunoglobulin G (IgG) antibody with high efficiency into the medium
Expression and secretion of a human IgG antibody by the diatom P. tricornutum Based on our previous studies on antibody expression in the ER of P. tricornutum [19], we expressed the human IgG antibody against the Hepatitis B Virus surface protein (CL4mAb) without the ER retention signal (DDEL) at the C-terminus of both antibody chains
Summary
There are many different expression systems for recombinant production of pharmaceutical proteins, many of these suffer from drawbacks such as yield, cost, complexity of purification, and possible contamination with human pathogens. Within the last decade microalgae came into focus of fuel industry as a renewable and beneficial source of lipid interesting for biodiesel production [3,4,5]. Another aspect of algal biotechnology is the idea of using microalgae as expression systems for recombinant proteins [6,7,8,9]. Hormones, antibodies or biotechnological relevant protein compounds – today there is a great demand for recombinant proteins. The introduction of the bacterial PHB-pathway led to efficient production of the bioplastic poly-3-hydroxybutyrate (PHB) demonstrating that algae might represent an production platform for proteins and other bioproducts [20]
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