Guidelines to cell engineering for monoclonal antibody production

Rita Costa, A.; Elisa Rodrigues, M.; Henriques, Mariana; Azeredo, Joana; Oliveira, Rosário

doi:10.1016/j.ejpb.2009.10.002

Cited by 178Viral Infectious Diseases and Gene Expression in InsectsMonoclonal and Polyclonal Antibodies ResearchProtein purification and stability

Guidelines to cell engineering for monoclonal antibody production

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Rita Costa, A., Elisa Rodrigues, M., Henriques, Mariana, Azeredo, Joana, Oliveira, Rosário·2010·European Journal of Pharmaceutics and Biopharmaceutics

DOI 10.1016/j.ejpb.2009.10.002

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Abstract

Monoclonal antibodies (mAbs) are currently used for many diagnostic and therapeutic applications. The high demand for these biopharmaceuticals has led to the development of large-scale manufacturing processes, with productivity improvements being mainly achieved by optimization of bioreactor systems. However, more recently, the early steps of production, previous to bioreactor culture, have been presented as alternative areas where productivity enhancements can be achieved. Thus, this review describes the progress made for the improvement of productivity in mammalian expression systems for the high production of mAbs. Advances in the development of mAb-producing cell lines are being made, particularly regarding expression vector design and methods used for transfection, with the intent to create a reproducible methodology. Selection of the most suitable clones is also a critical step that can be improved, by including variables other than the expression level, which is still the common practice. Furthermore, strategies of cell engineering, although still mostly based on trial-and-error experimentation and not in standard protocols, hold great interest to improve cell growth and productivity, as well as product quality in the future. Improvements of the initial steps of the production process would not only result in cells with higher expression ability, but would also speed-up the process development.

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Transient expression is ideal for high throughput screening for hits identification and very helpful for early stage product characterization.
“Yet, it is ideal for high throughput screening for hits identification and very helpful for early stage product characterization (Ozturk and Hu, 2005;Rosser et al., 2005;Rita Costa et al., 2010).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Rita Costa et al., 2010
By skipping the lengthy selection process for cells that have integrated the plasmid within their genome, transient transfection is much faster.
“By skipping the lengthy selection process for the cells that have integrated the plasmid within their genome, transient transfection is much faster (Rita Costa et al., 2010).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Rita Costa et al., 2010
For stable expression, a gene marker is usually integrated in the expression plasmid along with the cDNA encoding the gene of interest, conferring a selective advantage to cells that integrate the plasmid into their genome.
“For stable expression, a gene marker is usually integrated in the expression plasmid along with the cDNA encoding the gene of interest, conferring a selective advantage to the cells that integrate the plasmid into their genome (Rita Costa et al., 2010).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Rita Costa et al., 2010

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From Efficiency to Yield: Exploring Recent Advances in CHO Cell Line Development for Monoclonal Antibodies
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Attenuated glutamine synthetase as a selection marker in CHO cells to efficiently isolate highly productive stable cells for the production of antibodies and other biologics
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Exposure of a Monoclonal Antibody, IgG1, to UV-Light Leads to Protein Dithiohemiacetal and Thioether Cross-Links: A Role for Thiyl Radicals?
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Modulating secretory pathway pH by proton channel co‐expression can increase recombinant protein stability in plants
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Vector and Cell Line Engineering Technologies Toward Recombinant Protein Expression in Mammalian Cell Lines
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RETRACTED ARTICLE: Impact of different promoters, promoter mutation, and an enhancer on recombinant protein expression in CHO cells
Wang, W., Jia, Y., Li, Y.-C., Jing, C., Guo, X. H., Shang, X., Zhao, C., & Wang, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-10966-y · Cited by 28 · see citing works
Retracted
Generation of recombinant hyperimmune globulins from diverse B-cell repertoires
Keating, S. M., Mizrahi, R. A., Adams, M. S., Asensio, M. A., Benzie, E., Carter, K. P., Chiang, Y., Edgar, R. C., Gautam, B. K., Gras, A., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-00894-8 · Cited by 28 · see citing works
Enhanced targeted DNA methylation of the CMV and endogenous promoters with dCas9-DNMT3A3L entails distinct subsequent histone modification changes in CHO cells
Marx, N., Dhiman, H., Schmieder, V., Freire, C. M., Ly, N. N., Klanert, G., & Borth, N. (2021) · Metabolic Engineering · doi:10.1016/j.ymben.2021.04.014 · Cited by 27 · see citing works
Identification and characterization of heavy metal-resistant bacteria selected from different polluted sources
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Evaluating the efficiency of CHEF and CMV promoter with IRES and Furin/2A linker sequences for monoclonal antibody expression in CHO cells
Ebadat, S., Ahmadi, S., Ahmadi, M., Nematpour, F., Barkhordari, F., Mahdian, R., Davami, F., & Mahboudi, F. (2017) · PLoS ONE · doi:10.1371/journal.pone.0185967 · Cited by 27 · see citing works
Scale-Up of Protein Purification: Downstream Processing Issues
Milne, J. J. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-913-0_5 · Cited by 26 · see citing works
Optimization of heterologous protein production in Chinese hamster ovary cells under overexpression of spliced form of human X-box binding protein
Gulis, G., Simi, K. C. R., de Toledo, R. R., Maranhão, A. Q., & Brígido, M. M. (2014) · BMC Biotechnology · doi:10.1186/1472-6750-14-26 · Cited by 26 · see citing works
Isolation of single cells for protein therapeutics using microwell selection and Surface Plasmon Resonance imaging
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Recombinant Antibody Production Using a Dual-Promoter Single Plasmid System
Carrara, S. C., Fiebig, D., Bogen, J. P., Grzeschik, J., Hock, B. M., & Kolmar, H. (2021) · Antibodies · doi:10.3390/antib10020018 · Cited by 22 · see citing works
Building blocks needed for mechanistic modeling of bioprocesses: A critical review based on protein production by CHO cells
González-Hernández, Y., & Perré, P. (2024) · Metabolic Engineering Communications · doi:10.1016/j.mec.2024.e00232 · Cited by 22 · see citing works
Advancement in recombinant protein production using a marine oxygen carrier to enhance oxygen transfer in a CHO-S cell line
Pape, F. L., Bossard, M., Dutheil, D., Rousselot, M., Polard, V., Férec, C., Leize‐Zal, E., Delépine, P., & Zal, F. (2015) · Artificial Cells Nanomedicine and Biotechnology · doi:10.3109/21691401.2015.1029632 · Cited by 22 · see citing works
Molecular engineering strategies and methods for the expression and purification of IgG1-based bispecific bivalent antibodies
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Biologic Therapy and Severe Asthma in Children
Russo, D., Filippo, P. D., Attanasi, M., Lizzi, M., Pillo, S. D., & Chiarelli, F. (2021) · Biomedicines · doi:10.3390/biomedicines9070760 · Cited by 22 · see citing works
Identifying and engineering promoters for high level and sustainable therapeutic recombinant protein production in cultured mammalian cells
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Efficient enrichment of high-producing recombinant Chinese hamster ovary cells for monoclonal antibody by flow cytometry
Okumura, T., Masuda, K., Watanabe, K., Miyadai, K., Nonaka, K., Yabuta, M., & Ōmasa, T. (2015) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2015.01.007 · Cited by 21 · see citing works
New Mammalian Expression Systems
Zhu, J., & Hatton, D. (2017) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2016_55 · Cited by 21 · see citing works
A paradigm use of monoclonal antibodies-conjugated nanoparticles in breast cancer treatment: current status and potential approaches
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Recent advances in recombinant protein production
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An arginase-based system for selection of transfected CHO cells without the use of toxic chemicals
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Clinically Approved Monoclonal Antibodies–based Immunotherapy: Association With Glycemic Control and Impact Role of Clinical Pharmacist for Cancer Patient Care
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Biological insights into the expression of translation initiation factors from recombinant CHOK1SV cell lines and their relationship to enhanced productivity
Mead, E. J., Masterton, R. J., Feary, M., Obrezanova, O., Zhang, L., Young, R., & Smales, C. M. (2015) · Biochemical Journal · doi:10.1042/bj20150928 · Cited by 18 · see citing works
A doubly auxotrophic CHO‐K1 cell line for the production of recombinant monoclonal antibodies
Zhang, Q., Jiang, B., Du, Z., & Chasin, L. A. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27367 · Cited by 18 · see citing works
Bridging the gap
Munro, T. P., Mahler, S. M., Huang, E. P., Chin, D. Y., & Gray, P. P. (2011) · mAbs · doi:10.4161/mabs.3.5.16968 · Cited by 17 · see citing works
Vector-related stratagems for enhanced monoclonal antibody production in mammalian cells
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Scale-Up of Protein Purification: Downstream Processing Issues
Milne, J. J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6412-3_5 · Cited by 17 · see citing works
Applications of low-intensity pulsed ultrasound to increase monoclonal antibody production in CHO cells using shake flasks or wavebags
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Ebola virus VP35 induces high-level production of recombinant TPL-2–ABIN-2–NF-κB1 p105 complex in co-transfected HEK-293 cells
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Authors: Rita Costa, A., Elisa Rodrigues, M., Henriques, M., Azeredo, J., & Oliveira, R.
Affiliations: Institute for Biotechnology and Bioengineering (PT)
Corresponding author: Henriques, Mariana
ORCID: Henriques, Mariana
Azeredo, Joana
Venue: European Journal of Pharmaceutics and Biopharmaceutics
Publisher: Elsevier BV
Published: 2010-02
Volume: 74
Issue: 2
Pages: 127-138
ISSN: 0939-6411 (ISSN-L)
DOI: 10.1016/j.ejpb.2009.10.002
OpenAlex: W2108422551
Cited by: 178
References: 220
Citations by year: 2026: 2 · 2025: 8 · 2024: 10 · 2023: 12 · 2022: 8 · 2021: 14 · 2020: 11 · 2019: 9 · 2018: 13 · 2017: 17 · 2016: 8 · 2015: 10 · 2014: 15 · 2013: 20 · 2012: 10
FWCI: 2.80
Type: journal article
Language: en
Open access: green
hdl.handle.net
Licence: other-oa
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: European Journal of Pharmaceutics and Biopharmaceutics (publishedVersion)
PubMed (publishedVersion)
RepositóriUM (Universidade do Minho) (submittedVersion, other-oa)
Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, cc-by-nc-nd)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Keywords: monoclonal antibodies, cell engineering, mammalian cell expression systems, expression vector design, transfection, clone selection, antibody productivity, biopharmaceutical manufacturing, cell growth
MeSH terms: Animals, Antibodies, Monoclonal, Biotechnology, Humans, Technology, Pharmaceutical, Transfection, Protein Engineering, Cell Culture Techniques

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Guidelines to cell engineering for monoclonal antibody production

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