BMC Biotechnology | |
Efficient expression of fusion human epidermal growth factor in tobacco chloroplasts | |
Research | |
Yunpeng Wang1  Jieying Fan1  Shaochen Xing1  Zhengyi Wei2  | |
[1] Institute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, 130033, Changchun, China;Institute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, 130033, Changchun, China;Maize Research Institute, Guangxi Academy of Agricultural Sciences, 530007, Nanning, China; | |
关键词: EGF; Chloroplast transformation; Tobacco; GFP; Molecular farming; | |
DOI : 10.1186/s12896-022-00771-5 | |
received in 2022-03-24, accepted in 2022-12-27, 发布年份 2022 | |
来源: Springer | |
【 摘 要 】
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− 1 of fresh leaf). The chloroplast-derived GFP-EGF was capable of increasing the cell viability of the NSLC cell line A549 and enhancing the phosphorylation level of the EGF receptor in the A549 cells.ConclusionTheexpression 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.
【 授权许可】
CC BY
© The Author(s) 2023
【 预 览 】
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【 参考文献 】
- [1]
- [2]
- [3]
- [4]
- [5]
- [6]
- [7]
- [8]
- [9]
- [10]
- [11]
- [12]
- [13]
- [14]
- [15]
- [16]
- [17]
- [18]
- [19]
- [20]
- [21]
- [22]
- [23]
- [24]
- [25]
- [26]
- [27]
- [28]
- [29]
- [30]
- [31]
- [32]
- [33]
- [34]
- [35]
- [36]
- [37]
- [38]
- [39]
- [40]
- [41]
- [42]
- [43]
- [44]
- [45]
- [46]
- [47]
- [48]
- [49]
- [50]
- [51]
- [52]
- [53]
- [54]
- [55]
- [56]
- [57]
- [58]
- [59]
- [60]
- [61]
- [62]
- [63]
- [64]
- [65]
- [66]
- [67]
- [68]
- [69]
- [70]
- [71]
- [72]
- [73]