ArticleBioengineered2016
Glyco-engineering for the production of recombinant IgA1 with distinct mucin-type O-glycans in plants.
Article in Bioengineered, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Production of recombinant IgA1 with defined mucin-type O-glycans inFrontiers in plant science · 2025Article
- Plant-made pharmaceuticals.Plant biotechnology (Tokyo, Japan) · 2024Article
- Expression Profiling and Glycan Engineering of IgG Subclass 1-4 inFrontiers in bioengineering and biotechnology · 2020Article
- IgA: Structure, Function, and Developability.Antibodies (Basel, Switzerland) · 2019Review
- Distinct Fcα receptorThe Journal of biological chemistry · 2019Article
- Advanced Plant-Based Glycan Engineering.Frontiers in bioengineering and biotechnology · 2018Review
- Transient co-expression with threePlant methods · 2018Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
IgA nephropathy (IgAN) is a common autoimmune disease that is characterized by formation and deposition of IgA1-containing immune complexes frequently leading to end-stage kidney disease. The IgA1 in these immune complexes carries aberrantly glycosylated O-glycans. In circulating IgA1 these galactose-deficient mucin-type O-glycans are bound by autoantibodies and thus, contribute to immune complex formation and pathogenesis. Even though the disease is associated with the overproduction of aberrant O-glycans on IgA1, specific structure-function-studies of mucin-type O-glycans are limited. Compared to other expression hosts, plants offer the opportunity for de novo synthesis of O-glycans on recombinant glycoproteins as they are lacking the mammalian O-glycosylation pathway. Recently, we demonstrated that Nicotiana benthamiana are suitable for the generation of distinct O-glycans on recombinant IgA1. Here, we expand our engineering repertoire by in planta generation of galactose-deficient and α2,6-sialylated O-glycans which are the prevailing glycans detected on IgA1 from patients with IgAN.
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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.