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Article ; Online: Blockage of undesirable endocytosis of recombinant human growth/differentiation factor-5 in Chinese hamster ovary cell cultures requires heparin analogs with specific chain lengths.

Kim, Mi Gyeom / Lee, Gyun Min

2021 Volume 16, Issue 10, Page(s) e2100227

Abstract: Cell surface heparan sulfate proteoglycan (HSPG)-mediated endocytosis lowers the yield of recombinant human bone morphogenetic proteins (rhBMPs), such as rhBMP-2 and rhBMP-4, from Chinese hamster ovary (CHO) cell cultures. Exogenous recombinant human ... ...

Abstract	Cell surface heparan sulfate proteoglycan (HSPG)-mediated endocytosis lowers the yield of recombinant human bone morphogenetic proteins (rhBMPs), such as rhBMP-2 and rhBMP-4, from Chinese hamster ovary (CHO) cell cultures. Exogenous recombinant human growth/differentiation factor-5 (rhGDF-5), a member of the BMP family, bound to cell surface HSPGs and was actively internalized into CHO cells. Knockdown of heparan sulfate (HS) synthesis enzymes in CHO cells revealed that the chain length and N-sulfation of HS affected the binding of rhGDF-5 to HSPGs and subsequent rhGDF-5 internalization. To increase product yield by minimizing rhGDF-5 internalization in recombinant CHO (rCHO) cell cultures, heparin, and dextran sulfate (DS) of various polysaccharide chain lengths, which are structural analogs of HS, were examined for blockage of rhGDF-5 internalization. Heparin fragments of four monosaccharides (MW of 1.2 kDa) and DS (MW of 15 kDa) did not inhibit rhGDF-5 internalization whereas unfractionated heparin and DS of 200 kDa could significantly inhibit it. Compared to the control cultures, supplementation with unfractionated heparin or DS of 200 kDa at 1 g L
MeSH term(s)	Animals ; CHO Cells ; Cell Culture Techniques ; Cell Differentiation ; Cricetinae ; Cricetulus ; Endocytosis ; Heparin ; Heparitin Sulfate ; Humans
Chemical Substances	Heparin (9005-49-6) ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2021-08-13
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2221885-3
ISSN	1860-7314 ; 1860-6768
ISSN (online)	1860-7314
ISSN	1860-6768
DOI	10.1002/biot.202100227
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Article ; Online: Enhancing the production of adeno-associated virus (AAV)2 and AAV9 with high full capsid ratio in HEK293 cells through design-of-experiment optimization of triple plasmid ratio.

Park, Sungje / Shin, Seunghyeon / Lee, Haeshin / Jang, Jae-Hyung / Lee, Gyun Min

Biotechnology journal

2024 Volume 19, Issue 3, Page(s) e2300667

Abstract: The recombinant adeno-associated virus (rAAV) vectors used in gene therapy are usually produced by transfecting three different plasmids (Adenoviral helper plasmid (pHelper), AAV rep/cap plasmids (pRepCap), and Transgene plasmid (pAAV-GOI)) into human ... ...

Abstract	The recombinant adeno-associated virus (rAAV) vectors used in gene therapy are usually produced by transfecting three different plasmids (Adenoviral helper plasmid (pHelper), AAV rep/cap plasmids (pRepCap), and Transgene plasmid (pAAV-GOI)) into human embryonic kidney 293 (HEK293) cells. However, the high proportion of unwanted empty capsids generated during rAAV production is problematic. To simultaneously enhance the genome titer and full capsid ratio, the ratio of the three plasmids transfected into HEK293 cells was optimized using design-of-experiment (DoE). AAV2 and AAV9, which have different production kinetics, were selected as cell-associated and secreted model AAVs, respectively. In 125 mL Erlenmeyer flasks, the genome titers of rAAV2 and rAAV9 at DoE-optimized plasmid weight ratios (pHelper:pRep2Cap2:pAAV-GOI = 1:3.52:0.50 for rAAV2 and pHelper:pRep2Cap9:pAAV-GOI = 1:1.44:0.27 for rAAV9) were 2.23-fold and 2.26-fold higher than those in the widely used plasmid weight ratio (1:1:1), respectively. In addition, compared with the plasmid ratio of 1:1:1, the relative VP3 band intensities of rAAV2 and rAAV9, which represent the relative empty capsid ratios, were reduced by 26% and 25%, respectively, at the DoE-optimized plasmid ratio. Reduced empty capsid ratios in the DoE-optimized plasmid ratios were also confirmed using transmission electron microscopy (TEM). Taken together, regardless of the AAV serotype, DoE-aided optimization of the triple plasmid ratio was found to be an efficient means of improving the production of rAAV with a high full capsid ratio.
MeSH term(s)	Humans ; Capsid ; HEK293 Cells ; Genetic Vectors/genetics ; Dependovirus/genetics ; Plasmids/genetics ; Capsid Proteins/genetics ; Parvovirinae/genetics
Chemical Substances	Capsid Proteins
Language	English
Publishing date	2024-02-23
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2221885-3
ISSN	1860-7314 ; 1860-6768
ISSN (online)	1860-7314
ISSN	1860-6768
DOI	10.1002/biot.202300667
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Article ; Online: Enhancing the production of recombinant human TGF-β1 through an understanding of TGF-β1 synthesis, signaling, and endocytosis in CHO cells.

Kim, Kyungsoo / Kim, Young Sik / Jang, Ju Woong / Lee, Gyun Min

Biotechnology journal

2023 Volume 19, Issue 1, Page(s) e2300269

Abstract: To enhance the production of recombinant human transforming growth factor-beta1 (rhTGF-β1) in Chinese hamster ovary (CHO) cells, rhTGF-β1 was first characterized for endocytosis, signaling pathway, and overall maturation process. The mature rhTGF-β1 used ...

Abstract	To enhance the production of recombinant human transforming growth factor-beta1 (rhTGF-β1) in Chinese hamster ovary (CHO) cells, rhTGF-β1 was first characterized for endocytosis, signaling pathway, and overall maturation process. The mature rhTGF-β1 used for clinical application was internalized into CHO cells and inhibited the growth of CHO cells in a dose-dependent manner. However, mature rhTGF-β1 was mostly produced in the form of latent rhTGF-β1 in cultures of recombinant CHO (rCHO) cells producing rhTGF-β1 (CHO-rhTGF-β1). The concentration of active mature rhTGF-β1 in the culture supernatant of CHO-rhTGF-β1 cells was not high enough to compromise yield. In addition, a significant amount of unprocessed precursors was produced by CHO-rhTGF-β1 cells. Overexpression of PACEsol, a soluble form of furin, in CHO-rhTGF-β1 cells was effective for the proteolytic cleavage of unprocessed precursors. The highest mature rhTGF-β1 concentration (6.4 μg mL
MeSH term(s)	Cricetinae ; Animals ; Humans ; Transforming Growth Factor beta1/genetics ; Transforming Growth Factor beta1/pharmacology ; Cricetulus ; CHO Cells ; Recombinant Proteins/metabolism ; Signal Transduction ; Endocytosis
Chemical Substances	Transforming Growth Factor beta1 ; Recombinant Proteins
Language	English
Publishing date	2023-11-27
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2221885-3
ISSN	1860-7314 ; 1860-6768
ISSN (online)	1860-7314
ISSN	1860-6768
DOI	10.1002/biot.202300269
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Article ; Online: Mitigating transcriptional bottleneck using a constitutively active transcription factor, VP16-CREB, in mammalian cells.

Yoon, Chansik / Baek, Kyoung Eun / Kim, Dongil / Lee, Gyun Min

Metabolic engineering

2023 Volume 80, Page(s) 33–44

Abstract: High-level expression of recombinant proteins in mammalian cells has long been an area of interest. Inefficient transcription machinery is often an obstacle in achieving high-level expression of recombinant proteins in mammalian cells. Synthetic ... ...

Abstract	High-level expression of recombinant proteins in mammalian cells has long been an area of interest. Inefficient transcription machinery is often an obstacle in achieving high-level expression of recombinant proteins in mammalian cells. Synthetic promoters have been developed to improve the transcription efficiency, but have achieved limited success due to the limited availability of transcription factors (TFs). Here, we present a TF-engineering approach to mitigate the transcriptional bottlenecks of recombinant proteins. This includes: (i) identification of cAMP response element binding protein (CREB) as a candidate TF by searching for TFs enriched in the cytomegalovirus (CMV) promoter-driven high-producing recombinant Chinese hamster ovary (rCHO) cell lines via transcriptome analysis, (ii) confirmation of transcriptional limitation of active CREB in rCHO cell lines, and (iii) direct activation of the transgene promoter by expressing constitutively active CREB at non-cytotoxic levels in rCHO cell lines. With the expression of constitutively active VP16-CREB, the production of therapeutic proteins, such as monoclonal antibody and etanercept, in CMV promoter-driven rCHO cell lines was increased up to 3.9-fold. VP16-CREB was also used successfully with synthetic promoters containing cAMP response elements. Taken together, this strategy to introduce constitutively active TFs into cells is a useful means of overcoming the transcriptional limitations in recombinant mammalian cells.
MeSH term(s)	Cricetinae ; Animals ; Humans ; Cyclic AMP Response Element-Binding Protein/genetics ; Cyclic AMP Response Element-Binding Protein/metabolism ; Etoposide ; CHO Cells ; Cricetulus ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Cytomegalovirus Infections ; Transcription, Genetic ; Transcriptional Activation
Chemical Substances	Cyclic AMP Response Element-Binding Protein ; Etoposide (6PLQ3CP4P3) ; Recombinant Proteins
Language	English
Publishing date	2023-09-12
Publishing country	Belgium
Document type	Journal Article
ZDB-ID	1470383-x
ISSN	1096-7184 ; 1096-7176
ISSN (online)	1096-7184
ISSN	1096-7176
DOI	10.1016/j.ymben.2023.09.005
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Article ; Online: Genome-wide CRISPR/Cas9 knockout screening to mitigate cell growth inhibition induced by histone deacetylase inhibitors in recombinant CHO cells.

Kim, Dongil / Kim, Su Hyun / Yoon, Chansik / Lee, Gyun Min

Biotechnology and bioengineering

2023 Volume 121, Issue 3, Page(s) 931–941

Abstract: Histone deacetylase inhibitors (iHDACs) have been extensively studied as enhancers of therapeutic protein production in recombinant Chinese hamster ovary (CHO) (rCHO) cell cultures. However, the addition of iHDACs reduces the viable cell concentration ( ... ...

Abstract	Histone deacetylase inhibitors (iHDACs) have been extensively studied as enhancers of therapeutic protein production in recombinant Chinese hamster ovary (CHO) (rCHO) cell cultures. However, the addition of iHDACs reduces the viable cell concentration (VCC) in rCHO cell cultures, thereby reducing their potential to enhance therapeutic protein production. To mitigate the negative effects of iHDACs on VCC, screening using a clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR-associated protein 9 (Cas9)-based single-gene knockout (KO) library in rCHO cells was performed in the presence of CI994, a member of iHDACs, and 10 potential KO genes that enhanced the VCC of CI994-treated rCHO cells were identified. Among these, Bcor was validated as a promising KO target that improved VCC without negatively affecting the specific productivity in the presence of CI994. Bcor KO increased the VCC and therapeutic protein concentrations in both batch and fed-batch cultures in the presence of CI994. Taken together, these findings highlight the potential of the whole-genome CRISPR/Cas9-based single-gene KO cell library to identify KO target genes for the development of iHDAC-resistant rCHO cells for enhanced therapeutic protein production.
MeSH term(s)	Cricetinae ; Animals ; Cricetulus ; CHO Cells ; CRISPR-Cas Systems ; Histone Deacetylase Inhibitors/pharmacology ; Cell Proliferation
Chemical Substances	Histone Deacetylase Inhibitors
Language	English
Publishing date	2023-11-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	280318-5
ISSN	1097-0290 ; 0006-3592
ISSN (online)	1097-0290
ISSN	0006-3592
DOI	10.1002/bit.28611
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Article ; Online: Improving bone morphogenetic protein (BMP) production in CHO cells through understanding of BMP synthesis, signaling and endocytosis.

Kim, Kyungsoo / Kim, Mi Gyeom / Lee, Gyun Min

Biotechnology advances

2022 Volume 62, Page(s) 108080

Abstract: Bone morphogenetic proteins (BMPs) are a group of growth factors with the clinical potential to regulate cartilage and bone formation. Functionally active mature recombinant human BMPs (rhBMPs), produced primarily in Chinese hamster ovary (CHO) cells for ...

Abstract	Bone morphogenetic proteins (BMPs) are a group of growth factors with the clinical potential to regulate cartilage and bone formation. Functionally active mature recombinant human BMPs (rhBMPs), produced primarily in Chinese hamster ovary (CHO) cells for clinical applications, are considered difficult to express because they undergo maturation processes, signaling pathways, or endocytosis. Although BMPs are a family of proteins with similar mature domain sequence identities, their individual properties are diverse. Thus, understanding the properties of individual rhBMPs is essential to improve rhBMP production in CHO cells. In this review, we discuss various approaches to improve rhBMP production in CHO cells by understanding the overall maturation process, signaling pathways and endocytosis of individual rhBMPs.
MeSH term(s)	Cricetinae ; Animals ; Humans ; Cricetulus ; CHO Cells ; Bone Morphogenetic Proteins ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Endocytosis
Chemical Substances	Bone Morphogenetic Proteins ; Recombinant Proteins
Language	English
Publishing date	2022-12-13
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	47165-3
ISSN	1873-1899 ; 0734-9750
ISSN (online)	1873-1899
ISSN	0734-9750
DOI	10.1016/j.biotechadv.2022.108080
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Article ; Online: Small molecule epigenetic modulators for enhancing recombinant antibody production in CHO cell cultures.

Kim, Dongil / Yoon, Chansik / Lee, Gyun Min

Biotechnology and bioengineering

2022 Volume 119, Issue 3, Page(s) 820–831

Abstract: Small molecule epigenetic modulators that modify epigenetic states in cells are useful tools for regulating gene expression by inducing chromatin remodeling. To identify small molecule epigenetic modulators that enhance recombinant protein expression in ... ...

Abstract	Small molecule epigenetic modulators that modify epigenetic states in cells are useful tools for regulating gene expression by inducing chromatin remodeling. To identify small molecule epigenetic modulators that enhance recombinant protein expression in Chinese hamster ovary (CHO) cells, we examined eight histone deacetylase inhibitors (iHDACs) and six DNA methyltransferase inhibitors as chemical additives in recombinant CHO (rCHO) cell cultures. Among these, a benzamide-based iHDAC, CI994, was the most effective in increasing monoclonal antibody (mAb) production. Despite suppressing cell growth, the addition of CI994 to mAb-expressing GSR cell cultures at 10 μM resulted in a 2.3-fold increase in maximum mAb concentration due to a 3.0-fold increase in specific mAb productivity (q
MeSH term(s)	Acetylation ; Animals ; Antibody Formation ; CHO Cells ; Cell Culture Techniques ; Cricetinae ; Cricetulus ; Epigenesis, Genetic
Language	English
Publishing date	2022-01-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	280318-5
ISSN	1097-0290 ; 0006-3592
ISSN (online)	1097-0290
ISSN	0006-3592
DOI	10.1002/bit.28013
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Article ; Online: Improving recombinant bone morphogenetic protein-4 (BMP-4) production by autoregulatory feedback loop removal using BMP receptor-knockout CHO cell lines.

Kim, Che Lin / Lee, Gyun Min

Metabolic engineering

2018 Volume 52, Page(s) 57–67

Abstract: A Chinese hamster ovary (CHO) cell line producing recombinant human bone morphogenetic protein-4 (rhBMP-4) (CHO-BMP-4), which expresses essential components of BMP signal transduction, underwent autocrine BMP-4 signaling. RNA seq analysis on CHO host ... ...

Abstract	A Chinese hamster ovary (CHO) cell line producing recombinant human bone morphogenetic protein-4 (rhBMP-4) (CHO-BMP-4), which expresses essential components of BMP signal transduction, underwent autocrine BMP-4 signaling. RNA seq analysis on CHO host cells (DG44) treated with rhBMP-4 (20 µg/mL) suggested that rhBMP-4 induced signaling in CHO cells could be a critical factor in limiting rhBMP-4 production and should be removed to improve rhBMP-4 production in recombinant CHO (rCHO) cells. The inhibition of autocrine BMP signaling in CHO-BMP-4 cells by the addition of LDN-193189, a chemical inhibitor of BMP receptor type I, significantly increased the mRNA expression levels of rhBMP-4. To establish BMP signaling-free host cells, a BMP receptor, the BMPRIA or BMPRII gene in DG44 cells, was knocked out using CRISPR/Cas9 gene-editing technology. Using three different knockout (KO) host cell lines as well as a DG44 wild-type (wt) cell line, rCHO cell clones producing rhBMP-4 were generated by a stepwise selection with increasing methotrexate concentrations. KO-derived clones showed a significantly higher maximum rhBMP-4 concentration than wt-derived clones in both batch and fed-batch cultures. Unlike wt-derived clones, KO-derived cell clones were able to produce higher amounts of hBMP-4 transcripts and proteins in the stationary phase of growth and did not experience growth inhibition induced by rhBMP-4. The mean maximum rhBMP-4 concentration of KO host-derived clones was approximately 2.4-fold higher than that of wt-derived clones (P < 0.05). Taken together, the disruption of BMP signaling in CHO cells by knocking out the BMP receptor significantly improved rhBMP-4 production.
MeSH term(s)	Animals ; Antimetabolites/pharmacology ; Bone Morphogenetic Protein 4/biosynthesis ; Bone Morphogenetic Protein 4/genetics ; Bone Morphogenetic Protein Receptors/antagonists & inhibitors ; Bone Morphogenetic Protein Receptors/genetics ; CHO Cells ; CRISPR-Cas Systems ; Cricetinae ; Cricetulus ; Feedback, Physiological ; Gene Expression Profiling ; Gene Knockout Techniques ; Homeostasis ; Methotrexate/pharmacology ; Pyrazoles/pharmacology ; Pyrimidines/pharmacology ; Recombinant Proteins
Chemical Substances	Antimetabolites ; Bone Morphogenetic Protein 4 ; LDN 193189 ; Pyrazoles ; Pyrimidines ; Recombinant Proteins ; Bone Morphogenetic Protein Receptors (EC 2.7.11.30) ; Methotrexate (YL5FZ2Y5U1)
Language	English
Publishing date	2018-11-14
Publishing country	Belgium
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1470383-x
ISSN	1096-7184 ; 1096-7176
ISSN (online)	1096-7184
ISSN	1096-7176
DOI	10.1016/j.ymben.2018.11.003
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Article: Recombinase-mediated cassette exchange-based screening of a CRISPR/Cas9 library for enhanced recombinant protein production in human embryonic kidney cells: Improving resistance to hyperosmotic stress

Shin, Seunghyeon / Kim, Su Hyun / Park, Jong-Ho / Lee, Jae Seong / Lee, Gyun Min

International Metabolic Engineering Society Metabolic engineering. 2022 July, v. 72

2022

Abstract: Targeted engineering of mammalian cells has been widely attempted to ensure the efficient production of therapeutic proteins with proper quality during bioprocesses. However, the identification of novel targets for cell engineering is labor-intensive and ...

Abstract	Targeted engineering of mammalian cells has been widely attempted to ensure the efficient production of therapeutic proteins with proper quality during bioprocesses. However, the identification of novel targets for cell engineering is labor-intensive and has not yet been fully substantiated. Here, we established a CRISPR/Cas9 library screening platform in human embryonic kidney (HEK293) cells based on guide RNA integration mediated by recombinase-mediated cassette exchange (RMCE) to interrogate gene function in a high-throughput manner. This platform was further advanced using a nuclear localization signal-tagged recombinase that increased RMCE efficiency by 4.8-fold. Using this platform, we identified putative target genes, such as CDK8, GAS2L1, and GSPT1, and their perturbation confers resistance to hyperosmotic stress that inhibits cell growth and induces apoptosis. Knockout of these genes in monoclonal antibody (mAb)-producing recombinant HEK293 (rHEK293) cells enhanced resistance to hyperosmotic stress-induced apoptosis, resulting in enhanced mAb production. In particular, GSPT1-knockout yielded 2.3-fold increase in maximum mAb concentration in fed-batch culture where hyperosmotic stress naturally occurs due to nutrient feeding. Taken together, this streamlined screening platform allows the identification of novel targets associated with hyperosmotic stress, enabling the development of stress-resistant cells producing recombinant proteins.
Keywords	CRISPR-Cas systems ; RNA ; apoptosis ; cell growth ; genes ; humans ; kidneys ; monoclonal antibodies ; protein synthesis ; recombinant proteins ; recombinases ; therapeutics
Language	English
Dates of publication	2022-07
Size	p. 247-258.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1470383-x
ISSN	1096-7184 ; 1096-7176
ISSN (online)	1096-7184
ISSN	1096-7176
DOI	10.1016/j.ymben.2022.03.017
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Article: Factors affecting the quality of therapeutic proteins in recombinant Chinese hamster ovary cell culture

Ha, Tae Kwang / Kim, Dongil / Kim, Che Lin / Grav, Lise Marie / Lee, Gyun Min

Biotechnology advances. 2022 Jan., Feb., v. 54

2022

Abstract: Chinese hamster ovary (CHO) cells are the most widely used mammalian host cells for the commercial production of therapeutic proteins. Fed-batch culture is widely used to produce therapeutic proteins, including monoclonal antibodies, because of its ... ...

Abstract	Chinese hamster ovary (CHO) cells are the most widely used mammalian host cells for the commercial production of therapeutic proteins. Fed-batch culture is widely used to produce therapeutic proteins, including monoclonal antibodies, because of its operational simplicity and high product titer. Despite technical advances in the development of culture media and cell cultures, it is still challenging to maintain high productivity in fed-batch cultures while also ensuring good product quality. In this review, factors that affect the quality attributes of therapeutic proteins in recombinant CHO (rCHO) cell culture, such as glycosylation, charge variation, aggregation, and degradation, are summarized and categorized into three groups: culture environments, chemical additives, and host cell proteins accumulated in culture supernatants. Understanding the factors that influence the therapeutic protein quality in rCHO cell culture will facilitate the development of large-scale, high-yield fed-batch culture processes for the production of high-quality therapeutic proteins.
Keywords	Cricetulus griseus ; biotechnology ; cell culture ; glycosylation ; protein value ; therapeutics
Language	English
Dates of publication	2022-01
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	47165-3
ISSN	0734-9750
ISSN	0734-9750
DOI	10.1016/j.biotechadv.2021.107831
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