Image_5_The B1 Domain of Streptococcal Protein G Serves as a Multi-Functional Tag for Recombinant Protein Production in Plants.jpg
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.
History
References
- https://doi.org//10.1002/ijc.11451
- https://doi.org//10.1016/j.pep.2005.11.021
- https://doi.org//10.3390/ijms10041552
- https://doi.org//10.3389/fpls.2018.01893
- https://doi.org//10.1016/j.biotechadv.2011.09.013
- https://doi.org//10.3390/ma9120994
- https://doi.org//10.1038/s41578-021-00399-395
- https://doi.org//10.1016/j.ab.2016.10.016
- https://doi.org//10.1038/s41592-019-0357-353
- https://doi.org//10.1002/biot.200700214
- https://doi.org//10.1073/pnas.0405904101
- https://doi.org//10.1099/mic.0.000599
- https://doi.org//10.1016/j.copbio.2006.06.003
- https://doi.org//10.3389/fimmu.2013.00217
- https://doi.org//10.1186/1475-2859-11-157
- https://doi.org//10.1002/biot.200800241
- https://doi.org//10.1007/s10969-005-9003-9007
- https://doi.org//10.1073/pnas.91.3.913
- https://doi.org//10.1016/0092-8674(95)90395-X
- https://doi.org//10.1371/journal.pone.0086482
- https://doi.org//10.1002/cpps.77
- https://doi.org//10.1021/bi0507940
- https://doi.org//10.1111/pbi.13040
- https://doi.org//10.1038/s41598-018-22860-22862
- https://doi.org//10.1093/nar/gkt864
- https://doi.org//10.3791/50521
- https://doi.org//10.1016/j.str.2004.06.012
- https://doi.org//10.3389/fpls.2017.00247
- https://doi.org//10.1111/pbi.13369
- https://doi.org//10.1002/jps.22293
- https://doi.org//10.1038/36626
- https://doi.org//10.1016/j.biotechadv.2011.03.008
- https://doi.org//10.1016/j.pep.2006.06.024
- https://doi.org//10.1016/j.copbio.2019.11.002
- https://doi.org//10.1016/j.jplph.2020.153359
- https://doi.org//10.3389/fpls.2019.00720
- https://doi.org//10.1110/ps.8.8.1643
- https://doi.org//10.1111/jipb.13141
- https://doi.org//10.1007/s10529-010-0326-325
- https://doi.org//10.1038/73796
- https://doi.org//10.1016/j.pep.2007.10.018
- https://doi.org//10.1038/s41598-017-12188-12188
- https://doi.org//10.1021/bc900434c
- https://doi.org//10.1038/nbt1026
- https://doi.org//10.1038/s41598-018-23024-y
- https://doi.org//10.1080/13102818.2016.1166984