ArticleBMC biotechnology2023
Efficient expression of fusion human epidermal growth factor in tobacco chloroplasts.
Article in BMC biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Developing downstream processes for the purification of recombinant proteins and small molecules from Nicotiana benthamiana biomass.Plant biotechnology journal · 2026Review
- Sustainable production of myoglobin meat protein in plant chloroplasts.Frontiers in plant science · 2026Article
- Beyond Purification: Evolving Roles of Fusion Tags in Biotechnology.Current issues in molecular biology · 2025Review
- Recent trends and advances in chloroplast engineering and transformation methods.Frontiers in plant science · 2025Review
- Production of functional human galectin-1 in transplastomic tobacco and simplified recovery via batch-mode purification.Frontiers in plant science · 2025Article
- Leveraging Walnut Somatic Embryos as a Biomanufacturing Platform for Recombinant Proteins and Metabolites.Biotech (Basel (Switzerland)) · 2024Article
- Advances in Subcellular Accumulation Design for Recombinant Protein Production in Tobacco.Biodesign research · 2024Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundChloroplast transformation is a robust technology for the expression of recombinant proteins. Various types of pharmaceutical proteins including growth factors have been reported in chloroplasts via chloroplast transformation approach at high expression levels. However, high expression of epidermal growth factor (EGF) in chloroplasts with the technology is still unavailable.
resultsThe present work explored the high-level expression of recombinant EGF, a protein widely applied in many clinical therapies, in tobacco chloroplasts. In this work, homoplastic transgenic plants expressing fusion protein GFP-EGF, which was composed of GFP and EGF via a linker, were generated. The expression of GFP-EGF was confirmed by the combination of green fluorescent observation and Western blotting. The achieved accumulation of the recombinant fusion GFP-EGF was 10.21 ± 0.27% of total soluble proteins (1.57 ± 0.05 g kg
conclusionThe expression of recombinant EGF in tobacco chloroplasts via chloroplast transformation method was achieved at considerable accumulation level. The attempt gives a good example for the application of chloroplast transformation technology in recombinant pharmaceutical protein production.
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