TY - JOUR
T1 - A fusion between domains of the human bone morphogenetic protein-2 and maize 27 kD γ-Zein accumulates to high levels in the endoplasmic reticulum without forming protein bodies in transgenic tobacco
AU - Ceresoli, Valentina
AU - Mainieri, Davide
AU - Del Fabbro, Massimo
AU - Weinstein, Roberto
AU - Pedrazzini, Emanuela
PY - 2016/3/24
Y1 - 2016/3/24
N2 - Human Bone Morphogenetic Protein-2 (hBMP2) is an osteoinductive agent physiologically involved in bone remodeling processes. A commercialized recombinant hBMP2 produced in mammalian cell lines is available in different clinical applications where bone regeneration is needed, but widespread use has been hindered due to an unfavorable cost/effective ratio. Protein bodies are very large insoluble protein polymers that originate within the endoplasmic reticulum by prolamine accumulation during the cereal seed development. The N-terminal domain of the maize prolamin 27 kD γ-zein is able to promote protein body biogenesis when fused to other proteins. To produce high yield of recombinant hBMP2 active domain (ad) in stably transformed tobacco plants we have fused it to the γ-zein domain. We show that this zein-hBMP2ad fusion is retained in the endoplasmic reticulum without forming insoluble protein bodies. The accumulation levels are above 1% of total soluble leaf proteins, indicating that it could be a rapid and suitable strategy to produce hBMP2ad at affordable costs.
AB - Human Bone Morphogenetic Protein-2 (hBMP2) is an osteoinductive agent physiologically involved in bone remodeling processes. A commercialized recombinant hBMP2 produced in mammalian cell lines is available in different clinical applications where bone regeneration is needed, but widespread use has been hindered due to an unfavorable cost/effective ratio. Protein bodies are very large insoluble protein polymers that originate within the endoplasmic reticulum by prolamine accumulation during the cereal seed development. The N-terminal domain of the maize prolamin 27 kD γ-zein is able to promote protein body biogenesis when fused to other proteins. To produce high yield of recombinant hBMP2 active domain (ad) in stably transformed tobacco plants we have fused it to the γ-zein domain. We show that this zein-hBMP2ad fusion is retained in the endoplasmic reticulum without forming insoluble protein bodies. The accumulation levels are above 1% of total soluble leaf proteins, indicating that it could be a rapid and suitable strategy to produce hBMP2ad at affordable costs.
KW - Bone morphogenetic protein 2
KW - Endoplasmic reticulum
KW - Plant factories
KW - Protein accumulation
KW - Protein bodies
KW - γ-zein
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U2 - 10.3389/fpls.2016.00358
DO - 10.3389/fpls.2016.00358
M3 - Article
AN - SCOPUS:84961743041
VL - 7
JO - Frontiers in Plant Science
JF - Frontiers in Plant Science
SN - 1664-462X
IS - MAR2016
M1 - 358
ER -