ArticlemAbs
Optimizing assembly and production of native bispecific antibodies by codon de-optimization.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Advancing codon language modeling with synonymous codon constrained masking.Nucleic acids research · 2026Article
- Systematic Evaluation of Vector Sequence Elements in Isogenic CHO Cells for Improved Antibody Production.ACS synthetic biology · 2026Article
- Codon deoptimization of multispecific biologics reduces mispairing during transient mammalian protein expression.Frontiers in bioengineering and biotechnology · 2026Article
- Design and engineering of bispecific antibodies: insights and practical considerations.Frontiers in bioengineering and biotechnology · 2024Review
- Developing a second-generation clinical candidate AAV vector for gene therapy of familial hypercholesterolemia.Molecular therapy. Methods & clinical development · 2021Article
- Vaccines for COVID-19.Clinical and experimental immunology · 2020Review
- Computational tools for modern vaccine development.Human vaccines & immunotherapeutics · 2020Review
- Design and Production of Bispecific Antibodies.Antibodies (Basel, Switzerland) · 2019Review
- Tuning Relative Polypeptide Expression to Optimize Assembly, Yield and Downstream Processing of Bispecific Antibodies.Antibodies (Basel, Switzerland) · 2018Article
- Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When production of bispecific antibodies requires the co-expression and assembly of three or four polypeptide chains, low expression of one chain can significantly limit assembly and yield. κλ bodies, fully human bispecific antibodies with native IgG structure, are composed of a common heavy chain and two different light chains, one kappa and one lambda. No engineering is applied to force pairing of the chains, thus both monospecific and bispecific antibodies are secreted in the supernatant. In this context, stoichiometric expression of the two light chains allows for maximal assembly of the bispecific antibody. In this study, we selected a κλ body with suboptimal characteristics due to low kappa chain expression. Codon optimization to increase expression of the kappa chain did not improve bispecific yield. Surprisingly, progressive introduction of non-optimal codons into the sequence of the lambda chain resulted in lowering its expression for an optimal tuning of the relative distribution of monospecific and bispecific antibodies. This codon de-optimization led to doubling of the κλ body yield. These results indicate that assembly of different proteins into a recombinant complex is an interconnected process and that reducing the expression of one polypeptide can actually increase the overall yield.
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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.