Tailoring translational strength using Kozak sequence variants improves bispecific antibody assembly and reduces product‐related impurities in CHO cells

2020 ◽  
Vol 117 (7) ◽  
pp. 1946-1960 ◽  
Author(s):  
Noelia Blanco ◽  
Ambrose J. Williams ◽  
Danming Tang ◽  
Dejin Zhan ◽  
Shahram Misaghi ◽  
...  
Keyword(s):  
Cho Cells ◽  
Bispecific Antibody ◽  
Sequence Variants ◽  
Kozak Sequence ◽  
Related Impurities

A cell line development strategy to improve a bispecific antibody expression purity in CHO cells

2020 ◽  
pp. 107857
Author(s):  
Mingjian Ding ◽  
Li Shen ◽  
Liang Xiao ◽  
Xiaohui Liu ◽  
Jianzhong Hu
Keyword(s):  
Cell Line ◽  
Development Strategy ◽  
Cho Cells ◽  
Bispecific Antibody ◽  
Cell Line Development ◽  
Antibody Expression ◽  
A Cell

Purification of TNFR-Fc produced in recombinant CHO cells: Characterization of product-related impurities

2015 ◽  
Vol 50 (8) ◽  
pp. 1313-1317 ◽  
Author(s):  
Kyung Hyun Min ◽  
Gyun Min Lee
Keyword(s):  
Cho Cells ◽  
Recombinant Cho Cells ◽  
Related Impurities

Glycosylation pattern of humanized IgG-like bispecific antibody produced by recombinant CHO cells

2009 ◽  
Vol 85 (3) ◽  
pp. 535-542 ◽  
Author(s):  
Wook-Dong Kim ◽  
Miwako Tokunaga ◽  
Hiroyuki Ozaki ◽  
Takuya Ishibashi ◽  
Kohsuke Honda ◽  
...  
Keyword(s):  
Cho Cells ◽  
Bispecific Antibody ◽  
Glycosylation Pattern ◽  
Recombinant Cho Cells

A pharmacology guided approach for setting limits on product-related impurities for bispecific antibody manufacturing

2018 ◽  
Vol 94 ◽  
pp. 19-25
Author(s):  
Sharmila Rajan ◽  
Junichiro Sonoda ◽  
Timothy Tully ◽  
Ambrose J. Williams ◽  
Feng Yang ◽  
...  
Keyword(s):  
Bispecific Antibody ◽  
Related Impurities

Metabolic engineering of CHO cells to prepare glycoproteins

2018 ◽  
Vol 2 (3) ◽  
pp. 433-442 ◽  
Author(s):  
Qiong Wang ◽  
Michael J. Betenbaugh
Keyword(s):  
Metabolic Engineering ◽  
Cho Cells ◽  
Genetic Manipulation ◽  
Chinese Hamster ◽  
Post Translational Modification ◽  
Effector Functions ◽  
Recombinant Glycoproteins ◽  
Production Platform ◽  
Chemical Inhibitors ◽  
Amino Acid Mutations

As a complex and common post-translational modification, N-linked glycosylation affects a recombinant glycoprotein's biological activity and efficacy. For example, the α1,6-fucosylation significantly affects antibody-dependent cellular cytotoxicity and α2,6-sialylation is critical for antibody anti-inflammatory activity. Terminal sialylation is important for a glycoprotein's circulatory half-life. Chinese hamster ovary (CHO) cells are currently the predominant recombinant protein production platform, and, in this review, the characteristics of CHO glycosylation are summarized. Moreover, recent and current metabolic engineering strategies for tailoring glycoprotein fucosylation and sialylation in CHO cells, intensely investigated in the past decades, are described. One approach for reducing α1,6-fucosylation is through inhibiting fucosyltransferase (FUT8) expression by knockdown and knockout methods. Another approach to modulate fucosylation is through inhibition of multiple genes in the fucosylation biosynthesis pathway or through chemical inhibitors. To modulate antibody sialylation of the fragment crystallizable region, expressions of sialyltransferase and galactotransferase individually or together with amino acid mutations can affect antibody glycoforms and further influence antibody effector functions. The inhibition of sialidase expression and chemical supplementations are also effective and complementary approaches to improve the sialylation levels on recombinant glycoproteins. The engineering of CHO cells or protein sequence to control glycoforms to produce more homogenous glycans is an emerging topic. For modulating the glycosylation metabolic pathways, the interplay of multiple glyco-gene knockouts and knockins and the combination of multiple approaches, including genetic manipulation, protein engineering and chemical supplementation, are detailed in order to achieve specific glycan profiles on recombinant glycoproteins for superior biological function and effectiveness.

1075: ATM Sequence Variants are Predictive of the Development of Erectile Dysfunction Among Patients Treated for Prostate Cancer with 125Iodine Brachytherapy

2005 ◽  
Vol 173 (4S) ◽  
pp. 291-292
Author(s):  
Jamie A. Cesaretti ◽  
Richard G. Stock ◽  
Nelson N. Stone ◽  
Steven Lehrer ◽  
David A. Atencio ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Erectile Dysfunction ◽  
Sequence Variants

The effects of quisqualate on the CHO cells with conditionally expressed NMDA receptors

2000 ◽  
Vol 38 ◽  
pp. S38
Author(s):  
K Ito
Keyword(s):  
Nmda Receptors ◽  
Cho Cells
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