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

Valentina Ceresoli, Davide Mainieri, Massimo Del Fabbro, Roberto Weinstein, Emanuela Pedrazzini

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Article number358
JournalFrontiers in Plant Science
Volume7
Issue numberMAR2016
DOIs
Publication statusPublished - Mar 24 2016

Keywords

  • Bone morphogenetic protein 2
  • Endoplasmic reticulum
  • Plant factories
  • Protein accumulation
  • Protein bodies
  • γ-zein

ASJC Scopus subject areas

  • Plant Science

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