The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Robust expression of a bioactive mammalian protein in Chlamydomonas chloroplast
Open accessAbstract
Summary: We have engineered the chloroplast of eukaryotic algae to produce a number of recombinant proteins, including human monoclonal antibodies, but, to date, have achieved expression to only 0.5% of total protein. Here, we show that, by engineering the mammalian coding region of bovine mammary‐associated serum amyloid (M‐SAA) as a direct replacement for the chloroplast psbA coding region, we can achieve expression of recombinant protein above 5% of total protein. Chloroplast‐expressed M‐SAA accumulates predominantly as a soluble protein, contains the correct amino terminal sequence and has little or no post‐translational modification. M‐SAA is found in mammalian colostrum and stimulates the production of mucin in the gut, acting in the prophylaxis of bacterial and viral infections. Chloroplast‐expressed and purified M‐SAA is able to stimulate mucin production in human gut epithelial cell lines. As Chlamydomonas reinhardtii is an edible alga, production of therapeutic proteins in this organism offers the potential for oral delivery of gut‐active proteins, such as M‐SAA.
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“Transformed Chlamydomonas reindhartii chloroplast accumulated 5% total soluble protein (TSP) of the mammary-associated serum amyloid A3 peptide, but its antimicrobial activity was not tested [80,81].”
From Biofuels from algae: Challenges and potential (2010) · cites this paper as [80]
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Biofuels from algae: Challenges and potential
Hannon, M., Gimpel, J., Tran, M., Rasala, B., & Mayfield, S. (2010) · Biofuels · doi:10.4155/bfs.10.44 · Cited by 813
Self-citationRenewable fuels from algae: An answer to debatable land based fuels
Singh, A., Nigam, P. S. N., & Murphy, J. D. (2010) · Bioresource Technology · doi:10.1016/j.biortech.2010.06.032 · Cited by 661
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Microalgae as a future food source
Torres-Tiji, Y., Fields, F. J., & Mayfield, S. P. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2020.107536 · Cited by 559
Self-citationEngineering Plastid Genomes: Methods, Tools, and Applications in Basic Research and Biotechnology
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Metadata
- Authors
- Manuell, A. L., Beligni, M. V., Elder, J. H., Siefker, D. T., Tran, M., Weber, A., McDonald, T. L., & Mayfield, S. P.
- Affiliations
- Scripps Research Institute (US)
- University of Nebraska Medical Center (US)
- Corresponding author
- Mayfield, Stephen P.
- Venue
- Plant Biotechnology Journal
- Publisher
- Wiley
- Published
- 2007-03-15
- Volume
- 5
- Issue
- 3
- Pages
- 402-412
- ISSN
- 1467-7644 (ISSN-L)
- 1467-7652
- OpenAlex
- W4206882711
- Cited by
- 154
- References
- 35
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 7 · 2023: 3 · 2022: 10 · 2021: 3 · 2020: 12 · 2019: 7 · 2018: 8 · 2017: 8 · 2016: 15 · 2015: 11 · 2014: 14 · 2013: 9 · 2012: 14
- FWCI
- 5.32
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Plant Biotechnology Journal (publishedVersion)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- U.S. Department of Energy (FG0302ER15313)
- University of Nebraska Medical Center
- National Institutes of Health
- U.S. Public Health Service (A1059614)
- National Institute of General Medical Sciences (R01GM054659)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Keywords
- Chlamydomonas reinhardtii, recombinant protein expression, intestinal epithelial cells, edible algae, post-translational modification, colostrum proteins
- MeSH terms
- Amino Acid Sequence, Serum Amyloid A Protein, Animals, Base Sequence, Cattle, Chloroplasts, Photosynthesis, Protein Processing, Post-Translational, Recombinant Proteins, Sequence Alignment, Chlamydomonas reinhardtii, Genome, Protozoan, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Algal Proteins, Organisms, Genetically Modified
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