English

Abstract

Plant molecular pharming is a promising concept based on the large-scale production of recombinant proteins encompassing antibodies, vaccines and enzymes for human or veterinary uses and treatments. This new branch of biopharmaceutical industry offers pratcical and safety advantages over other traditional production systems. In higher plants, the complex cellular machinery makes possible synthesis and posttranslational modifications of heterologous protein macromolecules. The limiting obstacle to using this plant system at industrial scale is most often the low yield of the recombinant proteins. To improve this production level, many studies have been focusing on the choice of plant species, tissues, organs and cell suspension cultures or various upstream and downstream constituents in the expression cassettes. Likewise, new engineering technologies in plant molecular pharming have emerged relying on the usefulness of using soybean agglutinin (SBA), hydrophobin, zein and elastin-like peptide tags which are employed to extract and purify recombinant proteins in some host systems and under the control, and as a part, of different expression cassettes. Known to be very useful tools in recombinant proteins linkers separate different domains or units of the heterologous gene and thereby keep the functionality of the protein of interest. Here, we compare computationally one tag SBA as a part of fusion with a pharmaceutical human protein ADA joint directly or by the specific flexible (GGGGS)3 liker. The in silico analysis focuses on the mRNAs stability and fusions of tagged and tagged-linked ADA recombinant proteins.