ArticlePloS one2012
3D domain swapping causes extensive multimerisation of human interleukin-10 when expressed in planta.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- Cytokine multimerization: when more is more and sometimes less.Nature reviews. Immunology · 2026Review
- Identification of β-galactosidases along the secretory pathway of Nicotiana benthamiana that collectively hamper engineering of galactose-extended glycans on recombinant glycoproteins.Plant biotechnology journal · 2026Article
- Plant-based production of a protective vaccine antigen against the bovine parasitic nematode Ostertagia ostertagi.Scientific reports · 2023Article
- Bacterial expression of a designed single-chain IL-10 prevents severe lung inflammation.Molecular systems biology · 2023Article
- β-Hexosaminidases Along the Secretory Pathway ofFrontiers in plant science · 2021Article
- Functional characterization of Schistosoma mansoni fucosyltransferases in Nicotiana benthamiana plants.Scientific reports · 2020Article
- Russell-Like Bodies in Plant Seeds Share Common Features With Prolamin Bodies and Occur Upon Recombinant Protein Production.Frontiers in plant science · 2019Article
- Article
- Verticillium dahliae LysM effectors differentially contribute to virulence on plant hosts.Molecular plant pathology · 2017Article
- Production and glyco-engineering of immunomodulatory helminth glycoproteins in plants.Scientific reports · 2017Article
- Re-evaluation of IL-10 signaling reveals novel insights on the contribution of the intracellular domain of the IL-10R2 chain.PloS one · 2017Article
- Human Alpha Galactosidases Transiently Produced inFrontiers in plant science · 2017Article
- Co-expression of the protease furin in Nicotiana benthamiana leads to efficient processing of latent transforming growth factor-β1 into a biologically active protein.Plant biotechnology journal · 2016Article
- The N-glycan on Asn54 affects the atypical N-glycan composition of plant-produced interleukin-22, but does not influence its activity.Plant biotechnology journal · 2016Article
- The Potato Nucleotide-binding Leucine-rich Repeat (NLR) Immune Receptor Rx1 Is a Pathogen-dependent DNA-deforming Protein.The Journal of biological chemistry · 2015Article
- Transient Expression of Secretory IgA In Planta is Optimal Using a Multi-Gene Vector and may be Further Enhanced by Improving Joining Chain Incorporation.Frontiers in plant science · 2015Article
- Identification, Characterization and Down-Regulation of Cysteine Protease Genes in Tobacco for Use in Recombinant Protein Production.PloS one · 2015Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heterologous expression platforms of biopharmaceutical proteins have been significantly improved over the last decade. Further improvement can be established by examining the intrinsic properties of proteins. Interleukin-10 (IL-10) is an anti-inflammatory cytokine with a short half-life that plays an important role in re-establishing immune homeostasis. This homodimeric protein of 36 kDa has significant therapeutic potential to treat inflammatory and autoimmune diseases. In this study we show that the major production bottleneck of human IL-10 is not protein instability as previously suggested, but extensive multimerisation due to its intrinsic 3D domain swapping characteristic. Extensive multimerisation of human IL-10 could be visualised as granules in planta. On the other hand, mouse IL-10 hardly multimerised, which could be largely attributed to its glycosylation. By introducing a short glycine-serine-linker between the fourth and fifth alpha helix of human IL-10 a stable monomeric form of IL-10 (hIL-10(mono)) was created that no longer multimerised and increased yield up to 20-fold. However, hIL-10(mono) no longer had the ability to reduce pro-inflammatory cytokine secretion from lipopolysaccharide-stimulated macrophages. Forcing dimerisation restored biological activity. This was achieved by fusing human IL-10(mono) to the C-terminal end of constant domains 2 and 3 of human immunoglobulin A (Fcα), a natural dimer. Stable dimeric forms of IL-10, like Fcα-IL-10, may not only be a better format for improved production, but also a more suitable format for medical applications.
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