Molecular farming

Molecular Farming. Edited by Rainer Fischer, Stefan Schillberg... 

M.-A. DAoust, U. Busse, M. Martel et al., Alfalfa An efficient bioreactor for continuous recombinant protein production, in Molecular Farming of Plants and Animals for Human and Veterinary Medicine. 2003, eds. L. Erickson,... 

Molecular Farming. Edited by Rainer Fischer, Stefan Schillberg Copyright 2004 WILEY-VCH Verlag GmbH Co. KGaA, Weinheim ISBN 3-527-30786-9... 

The first proteins from transgenic plants to reach commercial status were avidin and P-glucuronidase (GUS) both of which are used as diagnostic agents in molecular biology. An important principle demonstrated by these case studies is that molecular farming in cereals can be an economical alternative even when the natural source of a protein is abundant (i.e. egg whites for avidin, and Escherichia coli for GUS) and where a market is already established. 

As discussed above, wheat has been used only rarely for molecular farming. Thus far, the only example of a pharmaceutical protein produced in wheat is a single chain Fv antibody, which was expressed using the Ubil promoter and achieved a maximum expression level of 1.5 pg g 1 dry weight [77]. Transgenic wheat producing Aspergillus phytase has also been reported [78]. 

Canadian Food Inspection Agency. Interim amendment to DIR2000-07 for confined research field trials of PNTs for plant molecular farming. 

When sufficiently high levels of expression and protein accumulation are achieved, efficient downstream processing protocols must be developed to insure product quality and the economic feasibility of production. As the demand for safe, recombinant pharmaceutical proteins continues to expand, the market potential of plant-produced recombinant proteins is considerable. Molecular farming can produce recombinant proteins at a lower cost than traditional expression systems based on microbial or animal cell culture, and without the risk of contamination with human pathogens. 

In order to make molecular farming commercially profitable, recombinant proteins must be produced at a sufficiently high yield and in an active form. It has become clear that, for high-level protein accumulation, the stability of transgene expression can be as important as the expression level itself. The quantity of protein is determined by the rate of protein synthesis, assembly as well as proteolytic degradation [83]. 

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