ArticleProceedings of the National Academy of Sciences of the United States of America2016
Engineering of complex protein sialylation in plants.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 107 citations in OpenAlex.
- Plant-Based Systems for Producing Therapeutic Proteins: Current Status and Future Prospects.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Beyond Starch: Towards a Scalable Potato Platform for Molecular Farming.Plant biotechnology journal · 2026Review
- Polysialic Acid Synthesis on theACS omega · 2026Article
- In planta engineering of polysialylated glycoproteins using salmonid polysialyltransferases.Scientific reports · 2026Article
- Review
- N-Glycoengineering of insect cells for tri-antennary N-glycan biosynthesis.Scientific reports · 2026Article
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- A plant cell-based platform for the expression of complex proteins with fucose-reduced sialylated N-glycans.Plant biotechnology journal · 2026Article
- CRISPR/Cas9-Mediated Knockouts of the ALG3 and GNTI in N. benthamiana and Their Application to Pharmaceutical Production.Plant biotechnology journal · 2025Article
- Trafficking and localization of Golgi-residentFrontiers in plant science · 2025Review
- Advances and challenges in plant N-glycoengineering: when fucosylation matters.Frontiers in plant science · 2025Review
- Fine-tuning the N-glycosylation of recombinant human erythropoietin using Chlamydomonas reinhardtii mutants.Plant biotechnology journal · 2024Article
- Plant-made pharmaceuticals.Plant biotechnology (Tokyo, Japan) · 2024Article
- Exploring the Potentiality of a Plant Platform for Monoclonal Antibody Production in Veterinary Medicine.Vaccines · 2024Article
- Efficient Expression of Functionally Active Aflibercept with Designed N-glycans.Antibodies (Basel, Switzerland) · 2024Article
- A genome-edited N. benthamiana line for industrial-scale production of recombinant glycoproteins with targeted N-glycosylation.Biotechnology journal · 2024Article
- Implications of O-glycan modifications in the hinge region of a plant-produced SARS-CoV-2-IgA antibody on functionality.Frontiers in bioengineering and biotechnology · 2024Article
- Killer to cure: Expression and production costs calculation of tobacco plant-made cancer-immune checkpoint inhibitors.Plant biotechnology journal · 2023Article
- Neuroimmunomodulatory properties of polysialic acid.Glycoconjugate journal · 2023Review
- Producing Biologics with Defined N-Glycosylation in Plants.Methods in molecular biology (Clifton, N.J.) · 2023Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
15 authors at 4 institutions in 2 countries.
Funding
Abstract
Sialic acids (Sias) are abundant terminal modifications of protein-linked glycans. A unique feature of Sia, compared with other monosaccharides, is the formation of linear homo-polymers, with its most complex form polysialic acid (polySia). Sia and polySia mediate diverse biological functions and have great potential for therapeutic use. However, technological hurdles in producing defined protein sialylation due to the enormous structural diversity render their precise investigation a challenge. Here, we describe a plant-based expression platform that enables the controlled in vivo synthesis of sialylated structures with different interlinkages and degree of polymerization (DP). The approach relies on a combination of stably transformed plants with transient expression modules. By the introduction of multigene vectors carrying the human sialylation pathway into glycosylation-destructed mutants, transgenic plants that sialylate glycoproteins in α2,6- or α2,3-linkage were generated. Moreover, by the transient coexpression of human α2,8-polysialyltransferases, polySia structures with a DP >40 were synthesized in these plants. Importantly, plant-derived polySia are functionally active, as demonstrated by a cell-based cytotoxicity assay and inhibition of microglia activation. This pathway engineering approach enables experimental investigations of defined sialylation and facilitates a rational design of glycan structures with optimized biotechnological functions.
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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.