ArticlePlant biotechnology journal2016
Co-expression of the protease furin in Nicotiana benthamiana leads to efficient processing of latent transforming growth factor-β1 into a biologically active protein.
Article in Plant biotechnology journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Protein-Derived Signal Peptides Induced by Agrobacterium Infection Promote the Secretion of Recombinant Proteins in Nicotiana benthamiana.Plant biotechnology journal · 2026Article
- Developing downstream processes for the purification of recombinant proteins and small molecules from Nicotiana benthamiana biomass.Plant biotechnology journal · 2026Review
- OsAPSE modulates non-covalent interactions between arabinogalactan proteinFrontiers in plant science · 2025Article
- Product safety aspects of plant molecular farming.Frontiers in bioengineering and biotechnology · 2023Review
- A plant-produced SARS-CoV-2 spike protein elicits heterologous immunity in hamsters.Frontiers in plant science · 2023Article
- SARS-CoV-2 spike trimer vaccine expressed in Nicotiana benthamiana adjuvanted with Alum elicits protective immune responses in mice.Plant biotechnology journal · 2022Article
- Augmenting glycosylation-directed folding pathways enhances the fidelity of HIV Env immunogen production in plants.Biotechnology and bioengineering · 2022Article
- Production of active Exendin-4 inFrontiers in plant science · 2022Article
- Production of Recombinant Active Human TGFβ1 inFrontiers in plant science · 2022Article
- Seed- and leaf-based expression of FGF21-transferrin fusion proteins for oral delivery and treatment of non-alcoholic steatohepatitis.Frontiers in plant science · 2022Article
- Plant-made dengue virus-like particles produced by co-expression of structural and non-structural proteins induce a humoral immune response in mice.Plant biotechnology journal · 2021Article
- Soluble Human Angiotensin- Converting Enzyme 2 as a Potential Therapeutic Tool for COVID-19 is Produced at High Levels InFrontiers in plant science · 2021Article
- Increased FURIN expression in rheumatoid arthritis patients and its anti-inflammatory effect.Journal of clinical laboratory analysis · 2020Article
- Recombinant production, purification, crystallization, and structure analysis of human transforming growth factor β2 in a new conformation.Scientific reports · 2019Article
- Production and Immunogenicity of Soluble Plant-Produced HIV-1 Subtype C Envelope gp140 Immunogens.Frontiers in plant science · 2019Article
- Production of Biopharmaceuticals inFrontiers in plant science · 2019Article
- Article
- Critical Evaluation of Strategies for the Production of Blood Coagulation Factors in Plant-Based Systems.Frontiers in plant science · 2019Review
- Production of complex viral glycoproteins in plants as vaccine immunogens.Plant biotechnology journal · 2018Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transforming growth factor beta (TGF-β) is a signalling molecule that plays a key role in developmental and immunological processes in mammals. Three TGF-β isoforms exist in humans, and each isoform has unique therapeutic potential. Plants offer a platform for the production of recombinant proteins, which is cheap and easy to scale up and has a low risk of contamination with human pathogens. TGF-β3 has been produced in plants before using a chloroplast expression system. However, this strategy requires chemical refolding to obtain a biologically active protein. In this study, we investigated the possibility to transiently express active human TGF-β1 in Nicotiana benthamiana plants. We successfully expressed mature TGF-β1 in the absence of the latency-associated peptide (LAP) using different strategies, but the obtained proteins were inactive. Upon expression of LAP-TGF-β1, we were able to show that processing of the latent complex by a furin-like protease does not occur in planta. The use of a chitinase signal peptide enhanced the expression and secretion of LAP-TGF-β1, and co-expression of human furin enabled the proteolytic processing of latent TGF-β1. Engineering the plant post-translational machinery by co-expressing human furin also enhanced the accumulation of biologically active TGF-β1. This engineering step is quite remarkable, as furin requires multiple processing steps and correct localization within the secretory pathway to become active. Our data demonstrate that plants can be a suitable platform for the production of complex proteins that rely on specific proteolytic processing.
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