Song Shi-Jian, Diao Hai-Ping, Moon Byeongho, Yun Areum, Hwang Inhwan
Department of Life Science, Pohang University of Science and Technology, Pohang, South Korea.
Front Plant Sci. 2022 Apr 25;13:878677. doi: 10.3389/fpls.2022.878677. eCollection 2022.
Plants have long been considered a cost-effective platform for recombinant production. A recently recognized additional advantage includes the low risk of contamination of human pathogens, such as viruses and bacterial endotoxins. Indeed, a great advance has been made in developing plants as a "factory" to produce recombinant proteins to use for biopharmaceutical purposes. However, there is still a need to develop new tools for recombinant protein production in plants. In this study, we provide data showing that the B1 domain of Streptococcal protein G (GB1) can be a multi-functional domain of recombinant proteins in plants. N-terminal fusion of the GB1 domain increased the expression level of various target proteins ranging from 1.3- to 3.1-fold at the protein level depending on the target proteins. GB1 fusion led to the stabilization of the fusion proteins. Furthermore, the direct detection of GB1-fusion proteins by the secondary anti-IgG antibody eliminated the use of the primary antibody for western blot analysis. Based on these data, we propose that the small GB1 domain can be used as a versatile tag for recombinant protein production in plants.
长期以来，植物一直被认为是重组生产的经济高效平台。最近认识到的一个额外优势是，其感染人类病原体（如病毒和细菌内毒素）的风险较低。事实上，在将植物开发成用于生产生物制药用途重组蛋白的“工厂”方面已经取得了巨大进展。然而，仍需要开发用于在植物中生产重组蛋白的新工具。在本研究中，我们提供的数据表明，链球菌蛋白G（GB1）的B1结构域可以成为植物中重组蛋白的多功能结构域。GB1结构域的N端融合使各种靶蛋白的表达水平在蛋白质水平上提高了1.3至3.1倍，具体取决于靶蛋白。GB1融合导致融合蛋白的稳定。此外，通过二抗抗IgG抗体直接检测GB1融合蛋白，无需使用一抗进行蛋白质印迹分析。基于这些数据，我们提出小GB1结构域可作为植物中重组蛋白生产的通用标签。
