Effect of culture pH on recombinant antibody production by a new human cell line, F2N78, grown in suspension at 33.0 °C and 37.0 °C

Seo, Jin Seok; Kim, Yeon Jung; Cho, Jong Moon; Baek, Eric; Lee, Gyun Min

doi:10.1007/s00253-013-4849-2

Cited by 25 publications

(13 citation statements)

References 32 publications

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“…Temperature had the largest significant effect on IgG titer via its effect on the production rate. However, the significance of the center point associated with IgG production rate suggests there exists an optimal temperature for maximizing IgG production so that using a temperature that is either too high or too low will reduce IgG production as has been well documented …”

Section: Resultsmentioning

confidence: 99%

Identifying a robust design space for glycosylation during monoclonal antibody production

Amand

Hayes

Radhakrishnan

et al. 2016

Biotechnology Progress

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Glycan distribution has been identified as a "critical quality attribute" for many biopharmaceutical products, including monoclonal antibodies. Consequently, determining quantitatively how process variables affect glycan distribution is important during process development to control antibody glycosylation. In this work, we assess the effect of six bioreactor process variables on the glycan distribution of an IgG1 produced in CHO cells. Our analysis established that glucose and glutamine media concentration, temperature, pH, agitation rate, and dissolved oxygen (DO) had small but significant effects on the relative percentage of various glycans. In addition, we assessed glycosylation enzyme transcript levels and intracellular sugar nucleotide concentrations within the CHO cells to provide a biological explanation for the observed effects on glycan distributions. From these results we identified a robust operating region, or design space, in which the IgG1 could be produced with a consistent glycan distribution. Since our results indicate that perturbations to bioreactor process variables will cause only small (even if significant) changes to the relative percentage of various glycans (<±1.5%)-changes that are too small to affect the bioactivity and efficacy of this IgG1 significantly-it follows that the glycan distribution obtained will be consistent even with relatively large variations in bioreactor process variables. However, for therapeutic proteins where bioactivity and efficacy are affected by small changes to the relative percentage of glycans, the same analysis would identify the manipulated variables capable of changing glycan distribution, and hence can be used to implement a glycosylation control strategy. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:1149-1162, 2016.

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Section: Resultsmentioning

confidence: 99%

Identifying a robust design space for glycosylation during monoclonal antibody production

Amand

Hayes

Radhakrishnan

et al. 2016

Biotechnology Progress

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“…The pH of hydrogels, prepared at optimum condition, was appropriately adjusted to be in the range of 7-7.5 as typical pH of 6.8 to 7.6 for cell culture [37] and pH of 7.0-7.4 for the highest specific growth rate [38]. Also, as shown in Figure 1c, a co-current coaxial needle was built in which the hydrogel precursor solution (plus cell in cellular investigations) flows through the external conduit and NaOH as a gellant passes through internal needle.…”

Section: Adjustment Of Hydrogel Ph and Instant Gel Formation On The Nmentioning

confidence: 99%

pH-Sensitive Chitosan Hydrogel with Instant Gelation for Myocardial Regeneration

Alimirzaei¹,

Vasheghani‐Farahani²,

Ghiaseddin³

et al. 2017

J Tissue Sci Eng

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“…A human fibrosacrcoma-derived cell line (HT-1080) can produce erythropoietin (EPO) with higher levels of tetra-antennary structures and none of the antigenic Neu5Gc is present (Shahrokh et al 2011). Fusion of 293 cells with a B-cell line (Namalwa cells) yielded a cell line useful in transient and stable clone production ) which produces antibody with more terminal galactose, similar to human plasma (Seo et al 2013). …”

Section: Cell Type Specific Glycosylationmentioning

confidence: 99%

Glycosylation in Cell Culture

Spearman

Butler

2014

Cell Engineering

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Glycosylation affects many general functional factors of a glycoprotein, such as stability, inhibition of proteolysis, solubility, aggregation, as well as other attributes critical to its use as a biotherapeutic. Therefore our understanding of the glycosylation pathway, factors that affect it, and our ability to manipulate glycosylation are essential in producing superior biotherapeutics. The complex synthetic pathway of N-linked glycosylation occurs in both the endoplasmic reticulum and Golgi and involves a large number of precursors and enzymes, leading to a large array of possible glycan structures. Thus, variability in glycosylation may be influenced by numerous factors that affect this pathway, such as host cell type, nutrient levels and supplements, dissolved oxygen, pH, temperature, and by-product accumulation, and thus must be closely monitored. Better analytical techniques have allowed linking specific glycan structures to functionality of glycoproteins, which have led to efforts to modify glycosylation through genetic engineering, sequence-interfering RNA (siRNA), glycosylation inhibitors or chemoenzymatic modification.

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Effect of culture pH on recombinant antibody production by a new human cell line, F2N78, grown in suspension at 33.0 °C and 37.0 °C

Cited by 25 publications

References 32 publications

Identifying a robust design space for glycosylation during monoclonal antibody production

Identifying a robust design space for glycosylation during monoclonal antibody production

pH-Sensitive Chitosan Hydrogel with Instant Gelation for Myocardial Regeneration

Glycosylation in Cell Culture

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