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Master Thesis

Analysis of a Tyrosine-and Lysine-Rich Fusion Protein Engineered for the Production of Cell Wall-Bound Recombinant Proteins

Abstract : C5a and IL6 are small proteins that are already industrially produced for pharmaceutical purposes by microbial fermentation. It was shown that producing them in stably transformed tobacco plants was possible as well. Going further, a new construct genetic construct addressing those proteins to the apoplast to bind and store them in the cell wall was made. This system was achieved using a fusion protein which included the TLRP (Tyrosine- and Lysine- Rich Protein). The purpose of this construct was to ease the purification process and reduce its cost. The yields and the actual localizations of the recombinant proteins that this technique could produce were then investigated in order to know if this system was working efficiently. Different lines, tissues and cellular localizations were investigated to find out the best that could be achieved out of this system. Some of the recombinant protein could, as expected, be recovered from the cell wall but no more than 50% of the whole production as most of the collected recombinant proteins remained free in the apoplast. The overall production of those plants was anyway low. The maximum yield of IL6 extracted from the cell wall being around 1 pg/mg of fresh weight for young leaves, which is the most promising tissue analyzed. A new construct using EGFP was as well prepared in order to further analyze this system
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Master Thesis
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Submitted on : Friday, November 28, 2014 - 11:15:22 AM
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  • HAL Id : dumas-01088584, version 1

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Nils Saillard. Analysis of a Tyrosine-and Lysine-Rich Fusion Protein Engineered for the Production of Cell Wall-Bound Recombinant Proteins. Agricultural sciences. 2013. ⟨dumas-01088584⟩

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