ArticleFrontiers in bioengineering and biotechnology2023
Codon optimization regulates IgG3 and IgM expression and glycosylation in
Article in Frontiers in bioengineering and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 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
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Light Chain Isotype and Antibody-Specificity Impact on Virus Neutralization.Antibodies (Basel, Switzerland) · 2025Article
- Modeling coding sequence design for virus-based expression in tobacco.Synthetic and systems biotechnology · 2025Article
- Investigating the impact of synonymous gene recoding on a recombinantly expressed monoclonal antibody under different process parameters.Bioengineering & translational medicine · 2025Article
- IgG1 versus IgG3: influence of antibody-specificity and allotypic variance on virus neutralization efficacy.Frontiers in immunology · 2024Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plants are being increasingly recognized for the production of complex human proteins, including monoclonal antibodies (mAbs). Various methods have been applied to boost recombinant expression, with DNA codon usage being an important approach. Here, we transiently expressed three complex human mAbs in Nicotiana benthamiana, namely one IgG3 and two IgM directed against SARS-CoV-2 as codon optimized(CO) and non-codon optimized (NCO) variants. qRT-PCR exhibited significantly increased mRNA levels of all CO variants compared to the non-codon optimized orthologues, in line with increased protein expression. Purified CO and NCO mAbs did not exhibit obvious biochemical differences, as determined by SDS-PAGE and antigen binding activities. By contrast, enhanced production selectively impacts on glycosite occupancy and N-glycan processing, with increased mannosidic structures. The results point to a careful monitoring of recombinant proteins upon enhancing expression. Especially if it comes to therapeutic application even subtle modifications might alter product efficacy or increase immunogenicity.
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Registered trials
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