ArticleBMC biotechnology2010
Engineering of N. benthamiana L. plants for production of N-acetylgalactosamine-glycosylated proteins--towards development of a plant-based platform for production of protein therapeutics with mucin type O-glycosylation.
Article in BMC biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 55 citations in OpenAlex.
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Highly efficient transgene-free ErCas12a RNP-protoplast genome editing and single-cell regeneration in Nicotiana benthamiana for glyco-engineering.Plant biotechnology journal · 2026Article
- 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
- Production of recombinant IgA1 with defined mucin-type O-glycans inFrontiers in plant science · 2025Article
- Plant-made pharmaceuticals.Plant biotechnology (Tokyo, Japan) · 2024Article
- Improving Protein Quantity and Quality-The Next Level of Plant Molecular Farming.International journal of molecular sciences · 2022Review
- Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021Article
- In Planta Production of the Receptor-Binding Domain From SARS-CoV-2 With Human Blood Group A Glycan Structures.Frontiers in chemistry · 2021Article
- Plant Platforms for Efficient Heterologous Protein Production.Biotechnology and bioprocess engineering : BBE · 2021Review
- A Novel CAR Expressing NK Cell Targeting CD25 With the Prospect of Overcoming Immune Escape Mechanism in Cancers.Frontiers in oncology · 2021Article
- A Roadmap for the Molecular Farming of Viral Glycoprotein Vaccines: Engineering Glycosylation and Glycosylation-Directed Folding.Frontiers in plant science · 2020Review
- Critical Evaluation of Strategies for the Production of Blood Coagulation Factors in Plant-Based Systems.Frontiers in plant science · 2019Review
- Characterization of the hypersensitive response-like cell death phenomenon induced by targeting antiviral lectin griffithsin to the secretory pathway.Plant biotechnology journal · 2018Article
- Advanced Plant-Based Glycan Engineering.Frontiers in bioengineering and biotechnology · 2018Review
- Transient co-expression with threePlant methods · 2018Article
- Production and glyco-engineering of immunomodulatory helminth glycoproteins in plants.Scientific reports · 2017Article
- Substrate Specificity and Inhibitor Sensitivity of Plant UDP-Sugar Producing Pyrophosphorylases.Frontiers in plant science · 2017Article
- TheFrontiers in plant science · 2017Article
- Glyco-engineering for biopharmaceutical production in moss bioreactors.Frontiers in plant science · 2014Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundMucin type O-glycosylation is one of the most common types of post-translational modifications that impacts stability and biological functions of many mammalian proteins. A large family of UDP-GalNAc polypeptide:N-acetyl-α-galactosaminyltransferases (GalNAc-Ts) catalyzes the first step of mucin type O-glycosylation by transferring GalNAc to serine and/or threonine residues of acceptor polypeptides. Plants do not have the enzyme machinery to perform this process, thus restricting their use as bioreactors for production of recombinant therapeutic proteins.
resultsThe present study demonstrates that an isoform of the human GalNAc-Ts family, GalNAc-T2, retains its localization and functionality upon expression in N. benthamiana L. plants. The recombinant enzyme resides in the Golgi as evidenced by the fluorescence distribution pattern of the GalNAc-T2:GFP fusion and alteration of the fluorescence signature upon treatment with Brefeldin A. A GalNAc-T2-specific acceptor peptide, the 113-136 aa fragment of chorionic gonadotropin β-subunit, is glycosylated in vitro by the plant-produced enzyme at the "native" GalNAc attachment sites, Ser-121 and Ser-127. Ectopic expression of GalNAc-T2 is sufficient to "arm" tobacco cells with the ability to perform GalNAc-glycosylation, as evidenced by the attachment of GalNAc to Thr-119 of the endogenous enzyme endochitinase. However, glycosylation of highly expressed recombinant glycoproteins, like magnICON-expressed E. coli enterotoxin B subunit:H. sapiens mucin 1 tandem repeat-derived peptide fusion protein (LTBMUC1), is limited by the low endogenous UDP-GalNAc substrate pool and the insufficient translocation of UDP-GalNAc to the Golgi lumen. Further genetic engineering of the GalNAc-T2 plants by co-expressing Y. enterocolitica UDP-GlcNAc 4-epimerase gene and C. elegans UDP-GlcNAc/UDP-GalNAc transporter gene overcomes these limitations as indicated by the expression of the model LTBMUC1 protein exclusively as a glycoform.
conclusionPlant bioreactors can be engineered that are capable of producing Tn antigen-containing recombinant therapeutics.
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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.