Optimization of inside and outside factors to improve recombinant protein yield in plant

Optimization of inside and outside factors to improve recombinant protein yield in plant The use of plant systems as factories for recombinant protein production became a prominent alternative for pharmaceutical industries due to their high potential for protein accumulation. In the last decades, the application of plants for protein production has gained more attention, as plants represent an economic strategy that leads to high levels of purified and active proteins for the pharmaceutical sector. Currently, FDA approval of the first generation of recombinant proteins produced in carrot cells, taliglucerase alfa, demonstrated that plant cells have a significant capacity to express complex proteins for therapeutic use. Although plant systems still have technical and economic barriers that require improvements in future years, the optimization of upstream and downstream components affecting protein accumulation is considered a key feature in the development of new pharmaceutical proteins. Therefore, an improvement of critical features, including transcription, translation and post-translational modifications, in plant cells could make plant systems a safe and economical alternative for biopharmaceutical production. Hence, in this review, the most recent advances influencing the upstream and downstream processes involved in recombinant protein accumulation in plant cells are described. We also discuss how plant systems are becoming the benchmark for the production of several biopharmaceuticals. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Cell, Tissue and Organ Culture Springer Journals

Optimization of inside and outside factors to improve recombinant protein yield in plant

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Publisher
Springer Netherlands
Copyright
Copyright © 2017 by Springer Science+Business Media Dordrecht
Subject
Life Sciences; Plant Sciences; Plant Physiology; Plant Genetics and Genomics; Plant Pathology
ISSN
0167-6857
eISSN
1573-5044
D.O.I.
10.1007/s11240-017-1240-5
Publisher site
See Article on Publisher Site

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