Recombinant protein production in a variety of Nicotiana hosts: A comparative analysis

Andrew Conley, Hong Zhu, Linda C. Le, Anthony M. Jevnikar, Byong H. Lee, Jim E. Brandle, Rima Menassa (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

60 Citations (Scopus)


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 languageEnglish
Pages (from-to)434-444
JournalPlant Biotechnology Journal
Issue number4
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed


  • molecular farming
  • recombinant protein production
  • transgenic plants
  • transient expression
  • erythropoietin
  • interleukin-10
  • alfa-amylase
  • Pseudomonas aeruginosa


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