Recombinant proteins, glycosylation

Genetic addition and supplementation needed to improve plant recombinant protein glycosylation... 

Zhang, F., Saarinen, M.A., Itle, L.J. et al. (2002) The effect of dissolved oxygen (DO) concentration on the glycosylation of recombinant protein produced by the insect cell-baculovirus expression system. Biotechnology and Bioengineering, 11 (2), 219-224. 

Brooks, S.A. (2004) Appropriate glycosylation of recombinant proteins for human use implications of choice of expression system. Molecular Biotechnology, 28 (3), 241-255. 

Studies have shown that plants can make biologically active recombinant proteins through both transgenic and transient expression approaches. Although the plant post-translational machinery is similar to that of mammalian cells, there are some notable differences, e.g. differences in glycosylation, particularly the absence of sia-lation, which may impact the activity of certain proteins. The absence of mammalian enzymes may prevent complex maturation processes that are critical for the biological activity of proteins such as insulin. Fortunately these shortcomings affect the activity of only a limited number of proteins. 

Mammalian cell suspension cultures are the preferred choice for large-scale recombinant protein production in stirred-tank bioreactors. The most widely used systems are Chinese hamster ovary (CHO) cells and the murine myeloma fines NSO and SP2/0. In half of the biological license approvals from 1996-2000, CHO cells were used for the production of monoclonal antibodies and other recombinant glycosylated proteins, including tPA (tissue plasminogen activator) and an IgGl fusion with the tumor necrosis factor (TNF) receptor, the latter marketed as Enbrel [7]. 

Component Other name Native protein (glycoprotein) (kDa) Recombinant protein (non-glycosylated) (kDa) Colonies stimulated Chromosomal location Produced by... 

Jenkins N. and Curling E.M. (1994), Glycosylation of recombinant proteins problems and prospects, Enzyme Microb. Technol. 16, 354—364. 

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