ArticleFrontiers in plant science2022
The B1 Domain of Streptococcal Protein G Serves as a Multi-Functional Tag for Recombinant Protein Production in Plants.
Article in Frontiers in plant science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 16 citations in OpenAlex.
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- Knocking Out Two Polyphenol Oxidase Genes Significantly Improves Recombinant Protein Purification in Nicotiana benthamiana.Plant biotechnology journal · 2026Article
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- Protein engineering strategies to optimise recombinant product synthesis and accumulation in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
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- Production of active human iduronate-2-sulfatase (IDS) enzyme in Nicotiana benthamiana.Scientific reports · 2024Article
- Boosting the toolbox for live imaging of translation.RNA (New York, N.Y.) · 2024Article
- Structure of saguaro cactus virus 3' translational enhancer mimics 5' cap for eIF4E binding.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Advances in Subcellular Accumulation Design for Recombinant Protein Production in Tobacco.Biodesign research · 2024Review
- SARS-CoV-2 spike trimer vaccine expressed in Nicotiana benthamiana adjuvanted with Alum elicits protective immune responses in mice.Plant biotechnology journal · 2022Article
- Production of active Exendin-4 inFrontiers in plant science · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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