Production of recombinant therapeutic proteins in human cells: current achievements and future perspectives
Abstract
Over the past 20 years the demand for recombinant proteins has increased significantly. Mammalian cell lines have been extensively used to produce recombinant proteins. This expression system offers several advantages over microbial systems, mammalian cells have the cellular machinery to promote the secretion of the recombinant product and the posttranslational modifications, like glycosylation that is present in many of recombinant therapeutic proteins in the market. Human cell lines have emerged as a new and powerful alternative for production of such products. These cells are able to produce recombinant proteins with posttranslational modifications more similar to their natural counterparts, producing proteins with human-like glycosylation pattern avoiding immunogenic reactions against epitopes nonhumans. This review presents the available human cell lines that can be used in pharmaceutical industry, the advantages of this expression system and the main efforts made in this field.
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HKB-11 cells have recently shown high-level protein production and α2,3 and α2,6-sialic acid linkages.
“It has recently showed high-level protein production and α2,3 and α2,6-sialic acid linkages (Picanco-Castro et al., 2013).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Picanco-Castro et al., 2013
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
- Authors
- Picanco-Castro, V., Biaggio, R., Cova, D., & Swiech, K.
- Affiliations
- Universidade de São Paulo (BR)
- Venue
- Protein & Peptide Letters
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2013-11
- Volume
- 20
- Issue
- 12
- Pages
- 1373-1381
- ISSN
- 0929-8665 (ISSN-L)
- OpenAlex
- W1996524348
- Cited by
- 34
- References
- 1
- Citations by year
- 2025: 2 · 2023: 3 · 2022: 1 · 2021: 1 · 2020: 4 · 2019: 3 · 2018: 5 · 2017: 7 · 2016: 4 · 2015: 2 · 2014: 2
- FWCI
- 1.19
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Protein and Peptide Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fundação de Amparo à Pesquisa do Estado de São Paulo
- U.S. Food and Drug Administration
- 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 › Biotechnology › Transgenic Plants and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- recombinant therapeutic proteins, human cell lines, mammalian cell expression systems, post-translational modification, glycosylation, immunogenicity, recombinant protein expression, pharmaceutical manufacturing
- MeSH terms
- Biotechnology, Cell Line, Glycosylation, Humans, Protein Processing, Post-Translational, Recombinant Proteins, Bioreactors
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