ArticleInternational journal of molecular sciences2016
Studies to Prevent Degradation of Recombinant Fc-Fusion Protein Expressed in Mammalian Cell Line and Protein Characterization.
Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- Stable Constitutive BiP Expression Prolongs Late-Stage GLP-1-Fc Accumulation in CHO Cells.Bioengineering (Basel, Switzerland) · 2026Article
- A Review on the Stability Challenges of Advanced Biologic Therapeutics.Pharmaceutics · 2025Review
- Impact of fed-batch process intensification on the productivity and product quality of two CHO cell lines expressing unique novel molecular format proteins.Bioprocess and biosystems engineering · 2024Article
- Recombinant therapeutic proteins degradation and overcoming strategies in CHO cells.Applied microbiology and biotechnology · 2024Review
- Manipulation of mRNA translation elongation influences the fragmentation of a biotherapeutic Fc-fusion protein produced in CHO cells.Biotechnology and bioengineering · 2022Article
- Population balance modelling captures host cell protein dynamics in CHO cell cultures.PloS one · 2022Article
- Optimized Production of Fc Fusion Proteins by Sortase Enzymatic Ligation.Industrial & engineering chemistry research · 2021Article
- Mapping the molecular basis for growth related phenotypes in industrial producer CHO cell lines using differential proteomic analysis.BMC biotechnology · 2021Article
- The Instability of Dimeric Fc-Fusions Expressed in Plants Can Be Solved by Monomeric Fc Technology.Frontiers in plant science · 2021Article
- Identification and CRISPR/Cas9 Inactivation of the C1s Protease Responsible for Proteolysis of Recombinant Proteins Produced in CHO Cells.Biotechnology and bioengineering · 2019Article
- Quantification of residual AEBSF-related impurities by reversed-phase liquid chromatography.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2019Article
- Anti-Tumor Activity and Pharmacokinetics of AP25-Fc Fusion Protein.International journal of medical sciences · 2019Article
- Engineering the hinge region of human IgG1 Fc-fused bispecific antibodies to improve fragmentation resistance.Scientific reports · 2018Article
- Hydrolysis-Kinetic Study of AEBSF, a Protease Inhibitor Used during Cell-Culture Processing of the HIV-1 Broadly Neutralizing Antibody CAP256-VRC25.26.Analytical chemistry · 2018Article
- Proteomic Analysis of Host Cell Protein Dynamics in the Culture Supernatants of Antibody-Producing CHO Cells.Scientific reports · 2017Article
- Addressing challenging impurities in fusion proteins: A comprehensive review and cost-effective strategy for HCP and low molecular weight species control.Biotechnology progressReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clipping of recombinant proteins is a major issue in animal cell cultures. A recombinant Fc-fusion protein, VEGFR1(D1-D3)-Fc expressed in CHOK1SV GS-KO cells was observed to be undergoing clippings in lab scale cultures. Partial cleaving of expressed protein initiated early on in cell culture and was observed to increase over time in culture and also on storage. In this study, a few parameters were explored in a bid to inhibit clipping in the fusion protein The effects of culture temperature, duration of culture, the addition of an anti-clumping agent, ferric citrate and use of protease inhibitor cocktail on inhibition of proteolysis of the Fc fusion were studied. Lowering of culture temperature from 37 to 30 °C alone appears to be the best solution for reducing protein degradation from the quality, cost and regulatory points of view. The obtained Fc protein was characterized and found to be in its stable folded state, exhibiting a high affinity for its ligand and also biological and functional activities.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.