Human cells: new platform for recombinant therapeutic protein production
Abstract
The demand for recombinant therapeutic proteins is significantly increasing. There is a constant need to improve the existing expression systems, and also developing novel approaches to face the therapeutic proteins demands. Human cell lines have emerged as a new and powerful alternative for the production of human therapeutic proteins because this expression system is expected to produce recombinant proteins with post translation modifications more similar to their natural counterpart and reduce the potential immunogenic reactions against nonhuman epitopes. Currently, little information about the cultivation of human cells for the production of biopharmaceuticals is available. These cells have shown efficient production in laboratory scale and represent an important tool for the pharmaceutical industry. This review presents the cell lines available for large-scale recombinant proteins production and evaluates critically the advantages of this expression system in comparison with other expression systems for recombinant therapeutic protein production.
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Using human cell lines for recombinant protein production would favor human-like glycosylation and warrant that proteins harbor at least non-immunogenic glycans.
“One way to favor human-like glycosylation would be to use human cell lines for recombinant protein production.This strategy would warrant that proteins harbor, if not the ideal glycosylation pattern, at least a non-immunogenic glycans (Swiech et al., 2012).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Swiech et al., 2012
Cites
Large-Scale transfection of mammalian cells for the fast production of recombinant protein
Pham, P. L., Kamen, A., & Durocher, Y. (2006) · Molecular Biotechnology · doi:10.1385/mb:34:2:225 · Cited by 236 · see citing works
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Therapeutic glycoprotein production in mammalian cells
Lalonde, M.-E., & Durocher, Y. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.028 · Cited by 296 · see citing works
Donadio-Andréi, S., Chikh, K., Heuclin, C., Kuczewski, E., Charrié, A., Gauchez, A.-S., & Ronin, C. (2017) · European Thyroid Journal · doi:10.1159/000449463 · Cited by 11 · see citing works
- Authors
- Swiech, K., Picanço-Castro, V., & Covas, D. T.
- Affiliations
- Universidade de São Paulo (BR)
- Corresponding author
- Swiech, Kamilla
- Venue
- Protein Expression and Purification
- Publisher
- Elsevier BV
- Published
- 2012-07
- Volume
- 84
- Issue
- 1
- Pages
- 147-153
- ISSN
- 1046-5928 (ISSN-L)
- OpenAlex
- W2079554839
- Cited by
- 178
- References
- 1
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 11 · 2023: 14 · 2022: 10 · 2021: 9 · 2020: 8 · 2019: 13 · 2018: 20 · 2017: 16 · 2016: 21 · 2015: 18 · 2014: 17 · 2013: 13 · 2012: 1
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Protein Expression and Purification (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Keywords
- recombinant therapeutic proteins, human cell lines, recombinant protein expression, post-translational modification, immunogenicity, biopharmaceuticals, large-scale cell culture
- MeSH terms
- Biotechnology, Cell Line, Humans, Recombinant Proteins, Bioreactors
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