Abstract
Although many different crop species have been used to produce a wide
range of vaccines, antibodies, biopharmaceuticals and industrial
enzymes, tobacco has the most established history for the production of
recombinant proteins. To further improve the heterologous protein yield
of tobacco platforms, transient and stable expression of four
recombinant proteins (i.e. human erythropoietin and interleukin‐10, an
antibody against Pseudomonas aeruginosa, and a hyperthermostable α‐amylase) was evaluated in numerous species and cultivars of Nicotiana. Whereas the transient level of recombinant protein accumulation varied significantly amongst the different Nicotiana plant hosts, the variety of Nicotiana
had little practical impact on the recombinant protein concentration in
stable transgenic plants. In addition, this study examined the growth
rate, amount of leaf biomass, total soluble protein levels and the
alkaloid content of the various Nicotiana varieties to establish the best plant platform for commercial production of recombinant proteins. Of the 52 Nicotiana varieties evaluated, Nicotiana tabacum
(cv. I 64) produced the highest transient concentrations of recombinant
proteins, in addition to producing a large amount of biomass and a
relatively low quantity of alkaloids, probably making it the most
effective plant host for recombinant protein production.
Original language | English |
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Pages (from-to) | 434-444 |
Journal | Plant Biotechnology Journal |
Volume | 9 |
Issue number | 4 |
DOIs | |
Publication status | Published - 2011 |
MoE publication type | A1 Journal article-refereed |
Keywords
- molecular farming
- recombinant protein production
- transgenic plants
- transient expression
- erythropoietin
- interleukin-10
- alfa-amylase
- Pseudomonas aeruginosa