ArticlePlant biotechnology journal2018
An oligosaccharyltransferase from Leishmania major increases the N-glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana.
Article in Plant biotechnology journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 57 citations in OpenAlex.
- The Oligosaccharyltransferase Catalytic Subunit PsSTT3B Is Required for Asexual Development and Pathogenicity inJournal of fungi (Basel, Switzerland) · 2026Article
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- The oligosaccharyltransferase subunit PsSTT3A regulates N-glycosylation and is critical for development and virulence of Phytophthora sojae.Science China. Life sciences · 2025Article
- Elucidation of the late steps in the glycan-dependent ERAD of soluble misfolded glycoproteins.The Plant journal : for cell and molecular biology · 2025Article
- Enhanced efficacy of glycoengineered rice cell-produced trastuzumab.Plant biotechnology journal · 2024Article
- Plant-derived Durvalumab variants show efficient PD-1/PD-L1 blockade and therapeutically favourable FcR binding.Plant biotechnology journal · 2024Article
- Efficient Expression of Functionally Active Aflibercept with Designed N-glycans.Antibodies (Basel, Switzerland) · 2024Article
- Improving theFrontiers in plant science · 2024Article
- Effect of plant produced Anti-hIL-6 receptor antibody blockade on pSTAT3 expression in human peripheral blood mononuclear cells.Scientific reports · 2023Article
- Characterization of PcSTT3B as a Key Oligosaccharyltransferase Subunit Involved in N-glycosylation and Its Role in Development and Pathogenicity ofInternational journal of molecular sciences · 2023Article
- An oligosaccharyltransferase fromFrontiers in plant science · 2023Article
- Impact of mutations on the plant-based production of recombinant SARS-CoV-2 RBDs.Frontiers in plant science · 2023Article
- A plant-produced SARS-CoV-2 spike protein elicits heterologous immunity in hamsters.Frontiers in plant science · 2023Article
- The tobacco GNTI stem region harbors a strong motif for homomeric protein complex formation.Frontiers in plant science · 2023Article
- Codon optimization regulates IgG3 and IgM expression and glycosylation inFrontiers in bioengineering and biotechnology · 2023Article
- Augmenting glycosylation-directed folding pathways enhances the fidelity of HIV Env immunogen production in plants.Biotechnology and bioengineering · 2022Article
- Transient Expression of Glycosylated SARS-CoV-2 Antigens inPlants (Basel, Switzerland) · 2022Review
- Improving Protein Quantity and Quality-The Next Level of Plant Molecular Farming.International journal of molecular sciences · 2022Review
- Transient proteolysis reduction ofFrontiers in plant science · 2022Article
- Comparative analysis of plant transient expression vectors for targeted N-glycosylation.Frontiers in bioengineering and biotechnology · 2022Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
N-glycosylation is critical for recombinant glycoprotein production as it influences the heterogeneity of products and affects their biological function. In most eukaryotes, the oligosaccharyltransferase is the central-protein complex facilitating the N-glycosylation of proteins in the lumen of the endoplasmic reticulum (ER). Not all potential N-glycosylation sites are recognized in vivo and the site occupancy can vary in different expression systems, resulting in underglycosylation of recombinant glycoproteins. To overcome this limitation in plants, we expressed LmSTT3D, a single-subunit oligosaccharyltransferase from the protozoan Leishmania major transiently in Nicotiana benthamiana, a well-established production platform for recombinant proteins. A fluorescent protein-tagged LmSTT3D variant was predominately found in the ER and co-located with plant oligosaccharyltransferase subunits. Co-expression of LmSTT3D with immunoglobulins and other recombinant human glycoproteins resulted in a substantially increased N-glycosylation site occupancy on all N-glycosylation sites except those that were already more than 90% occupied. Our results show that the heterologous expression of LmSTT3D is a versatile tool to increase N-glycosylation efficiency in plants.
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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.