TY - JOUR
T1 - Plants as bioreactors: A comparative study suggests that Medicago truncatula is a promising production system
AU - Abranches, R.
AU - Marcel, S.
AU - Arcalis, E.
AU - Altmann, F.
AU - Fevereiro, P.
AU - Stoger, E.
PY - 2005
Y1 - 2005
N2 - Plants are emerging as a promising alternative to conventional platforms for the large-scale production of recombinant proteins. This field of research, known as molecular farming, is developing rapidly and several plant-derived recombinant proteins are already in advanced clinical trials. However, the full potential of molecular farming can only be realized if we gain a fundamental understanding of biological processes regulating the production and accumulation of functional recombinant proteins in plants. Recent studies indicate that species- and tissue-specific factors as well as plant physiology can have a significant impact on the amount and quality of the recombinant product. More detailed comparative studies are needed for each product, including the analysis of expression levels, biochemical properties, in vitro activity and subcellular localization. In this review we include the first results from an extensive comparative study in which the highly glycosylated enzyme phytase (from the fungus Aspergillus niger) was produced in different plant species (including tobacco and the model legume Medicago truncatula). Special emphasis is placed on M. truncatula, whose leaves accumulated the highest levels of active phytase. We discuss the potential of this species as a novel production host.
AB - Plants are emerging as a promising alternative to conventional platforms for the large-scale production of recombinant proteins. This field of research, known as molecular farming, is developing rapidly and several plant-derived recombinant proteins are already in advanced clinical trials. However, the full potential of molecular farming can only be realized if we gain a fundamental understanding of biological processes regulating the production and accumulation of functional recombinant proteins in plants. Recent studies indicate that species- and tissue-specific factors as well as plant physiology can have a significant impact on the amount and quality of the recombinant product. More detailed comparative studies are needed for each product, including the analysis of expression levels, biochemical properties, in vitro activity and subcellular localization. In this review we include the first results from an extensive comparative study in which the highly glycosylated enzyme phytase (from the fungus Aspergillus niger) was produced in different plant species (including tobacco and the model legume Medicago truncatula). Special emphasis is placed on M. truncatula, whose leaves accumulated the highest levels of active phytase. We discuss the potential of this species as a novel production host.
KW - Phytase
KW - Recombinant proteins
KW - Medicago truncatula
KW - Molecular farming
UR - http://www.scopus.com/inward/record.url?eid=2-s2.0-25644440058&partnerID=MN8TOARS
U2 - 10.1016/j.jbiotec.2005.04.026
DO - 10.1016/j.jbiotec.2005.04.026
M3 - Article
SP - 121
EP - 134
JO - Journal of Biotechnology
JF - Journal of Biotechnology
SN - 0168-1656
ER -