ArticleAntibody therapeutics2022
Vector design for enhancing expression level and assembly of knob-into-hole based FabscFv-Fc bispecific antibodies in CHO cells.
Article in Antibody therapeutics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Article
- Impact of Cistron Topology and Bicistronic Vector Design in the piggyBac Transposon System for Improved Antibody Expression.Biotechnology journal · 2026Article
- Structural stability of symmetric bispecific antibodies: a case study showing potential compromise near linker regions.Scientific reports · 2026Article
- Optimizing co-expression strategies for the simultaneous display and secretion of monoclonal antibodies in CHO cells.Scientific reports · 2025Article
- A novel single-vector featuring bidirectional promoters for production of bispecific antibody against rabies virus.BMC biotechnology · 2025Article
- Sequence and Configuration of a Novel Bispecific Antibody Format Impacts Its Production Using Chinese Hamster Ovary (CHO) Cells.Biotechnology and bioengineering · 2025Article
- Development of BCMA-Targeted Bispecific Natural Killer Cell Engagers for Multiple Myeloma Treatment.Antibodies (Basel, Switzerland) · 2024Article
- Detection of host cell microprotein impurities in antibody drug products.Nature communications · 2024Article
- Investigation on environmental factors contributing to bispecific antibody stability and the reversal of self-associated aggregates.Bioresources and bioprocessing · 2024Article
- Design and engineering of bispecific antibodies: insights and practical considerations.Frontiers in bioengineering and biotechnology · 2024Review
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Two-armed FabscFv-Fc is a favoured bispecific antibody (BsAb) format due to its advantages of the conventional IgG structure. Production of FabscFv-Fc requires expression of three polypeptide chains, one light chain (LC), one heavy chain (HC) and a scFv fused to the Fc (scFvFc) at optimal ratios. Methods: We designed a set of internal ribosome entry site (IRES)-mediated multi-cistronic vectors tailoring to various expression ratios of the three polypeptides to study how the chain ratios affect the FabscFv-Fc production. Results: Expression of HC and scFvFc chains at 1:1 ratio and excess LC gave the highest yield of correctly assembled product. Compared to the use of IRES and multiple promoters, using 2A peptides for co-expression of the three polypeptides gave the highest titre and correctly assembled product. Conclusion: The results obtained in this work provide insights to the impacts of hetero-chain ratios on the BsAb production.
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Registered trials
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