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Engineering of complex protein sialylation in plants
Open accessAbstract
Significance: Sialic acid (Sia) residues are essential monosaccharides in mammals and confer multiple biological functions. Their precise generation is important for both structure–function studies and biotechnological applications. We describe a unique technology that enables the controlled generation of protein sialylation in Nicotiana benthamiana . The plant engineering approach relies on a combination of endogenous glycan deconstruction and the introduction of human sialylation capabilities. An arrangement of transgenic and transient expression modules resulted in the targeted synthesis of Sia structures in three different linkage types, reaching a polymerization degree exceeding 40 residues (polySia). Importantly, the obtained functional activities of polySia point to novel biotherapeutic applications. Our results highlight the exceptional flexibility of the plant-based expression platform for engineering complex posttranslational protein modifications.
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“The tobacco plant Nicotiana benthamiana expression system was genetically modified to carry the human-type sialylation pathway and to generate mono-and disialylated structures with α2,3 and α2,6 linkage (Kallolimath et al., 2016).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Kallolimath et al., 2016
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Metadata
- Authors
- Kallolimath, S., Castilho, A., Strasser, R., Grünwald-Gruber, C., Altmann, F., Strubl, S., Galuska, C. E., Zlatina, K., Galuska, S. P., Werner, S., Thiesler, H., Werneburg, S., Hildebrandt, H., Gerardy-Schahn, R., & Steinkellner, H.
- Affiliations
- BOKU University (AT)
- Department of Chemistry, University of Natural Resources and Life Sciences, 1190 Vienna, Austria;
- Justus-Liebig-Universität Gießen (DE)
- Nambawan Biotech GmbH, D-06120 Halle/Saale, Germany;
- Medizinische Hochschule Hannover (DE)
- Institute for Cellular Chemistry, Hannover Medical School, 30625 Hannover, Germany
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2016-07-21
- Volume
- 113
- Issue
- 34
- Pages
- 9498-9503
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5003249
- OpenAlex
- W2489417518
- Cited by
- 113
- References
- 59
- Citations by year
- 2026: 10 · 2025: 9 · 2024: 12 · 2023: 12 · 2022: 11 · 2021: 9 · 2020: 18 · 2019: 8 · 2018: 14 · 2017: 7 · 2016: 2
- FWCI
- 9.02
- Type
- journal article
- Language
- en
- Update notices
- correction (2017-05-01)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Informationszentrum Lebenswissenschaften (ZB MED) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (GA 1755/1-2)
- Österreichische Forschungsförderungsgesellschaft (822757)
- Austrian Science Fund (FWF L575-B13 and TRP 242-B20)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Keywords
- sialic acid, polysialic acid, plant-based expression systems, transient expression, degree of polymerization, glycoproteins, microglial activation, cytotoxicity
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