ArticleFrontiers in bioengineering and biotechnology2022
Comparative analysis of plant transient expression vectors for targeted N-glycosylation.
Article in Frontiers in bioengineering and biotechnology, 2022. 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, 14 citations in OpenAlex.
- A plant cell-based platform for the expression of complex proteins with fucose-reduced sialylated N-glycans.Plant biotechnology journal · 2026Article
- Architects of folding, editors of immunity: the strategic use ofFrontiers in immunology · 2026Article
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Harnessing Transient Expression Systems with Plant Viral Vectors for the Production of Biopharmaceuticals inInternational journal of molecular sciences · 2025Review
- Advances and challenges in plant N-glycoengineering: when fucosylation matters.Frontiers in plant science · 2025Review
- Improving theFrontiers in plant science · 2024Article
- A genome-edited N. benthamiana line for industrial-scale production of recombinant glycoproteins with targeted N-glycosylation.Biotechnology journal · 2024Article
- Glyco engineered pentameric SARS-CoV-2 IgMs show superior activities compared to IgG1 orthologues.Frontiers in immunology · 2023Article
- Codon optimization regulates IgG3 and IgM expression and glycosylation inFrontiers in bioengineering and biotechnology · 2023Article
- An oligosaccharyltransferase fromFrontiers in plant science · 2023Article
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
While plant-based transient expression systems have demonstrated their potency to rapidly express economically feasible quantities of complex human proteins, less is known about their compatibility with posttranslational modification control. Here we investigated three commonly used transient expression vectors, pEAQ, magnICON and pTra for their capability to express a multi-component protein with controlled and modified N-glycosylation. Cetuximab (Cx), a therapeutic IgG1 monoclonal antibody, which carries next to the conserved Fc an additional N-glycosylation site (GS) in the Fab-domain, was used as model. While pEAQ and pTra produce fully assembled Cx at similar levels in
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