Cyanobacterial Production of Biopharmaceutical and Biotherapeutic Proteins
Open accessAbstract
Efforts to express human therapeutic proteins in photosynthetic organisms have been described in the literature. Regarding microalgae, most of the research entailed a heterologous transformation of the chloroplast, but transformant cells failed to accumulate the desired recombinant proteins in high quantity. The present work provides methods and DNA construct formulations for over-expressing in photosynthetic cyanobacteria, at the protein level, human-origin bio-pharmaceutical and bio-therapeutic proteins. Proof-of-concept evidence is provided for the design and reduction to practice of “fusion constructs as protein overexpression vectors” for the generation of the bio-therapeutic protein interferon α-2 (IFN). IFN is a member of the Type I interferon cytokine family, well-known for its antiviral and anti-proliferative functions. Fusion construct formulations enabled accumulation of IFN up to 12% of total cellular protein in soluble form. In addition, the work reports on the isolation and purification of the fusion IFN protein and preliminary verification of its antiviral activity. Combining the expression and purification protocols developed here, it is possible to produce fairly large quantities of interferon in these photosynthetic microorganisms, generated from sunlight, CO2, and H2O.
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Betterle et al. engineered Synechocystis sp. PCC 6803 to express human interferon α-2 as a fusion protein; the recombinant protein accumulated in soluble form and showed preliminary antiviral activity.
“For example, Betterle et al. engineered Synechocystis sp. PCC 6803 to express human interferon α-2, a therapeutic cytokine with antiviral and anti-proliferative activity, as a fusion protein; the recombinant protein accumulated in soluble form and showed preliminary antiviral activity [188].”
From Cyanobacteria as a Photosynthetic Chassis for Metabolic Pathway Engineering with Heterologous Gene Expression (2026) · cites this paper as [188]
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References 68 · Cited by 33
- Authors
- Betterle, N., Hidalgo Martinez, D., & Melis, A.
- Affiliations
- University of California, Berkeley (US)
- Corresponding author
- Melis, Anastasios
- Venue
- Frontiers in Plant Science
- Publisher
- Frontiers Media SA
- Published
- 2020-03-03
- Volume
- 11
- Pages
- 237-237
- ISSN
- 1664-462X (ISSN-L)
- PMC
- PMC7062967
- OpenAlex
- W3010528248
- Cited by
- 33
- References
- 68
- Citations by year
- 2026: 6 · 2025: 6 · 2024: 7 · 2023: 6 · 2022: 5 · 2021: 3
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Plant Science (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Keywords
- cyanobacteria, recombinant protein expression, interferon alpha 2, fusion constructs, photosynthetic microorganisms, therapeutic proteins, biopharmaceutical proteins, protein purification, antiviral activity, heterologous expression
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