ArticleFrontiers in cell and developmental biology2020
Targeting of the C-Type Lectin Receptor Langerin Using Bifunctional Mannosylated Antigens.
Article in Frontiers in cell and developmental biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Calcium Competitive Inhibition of Langerin by Thiazolopyrimidinones.Journal of medicinal chemistry · 2025Article
- MUC1 Glycopeptide Vaccine Modified with a GalNAc Glycocluster Targets the Macrophage Galactose C-type Lectin on Dendritic Cells to Elicit an Improved Humoral Response.Journal of the American Chemical Society · 2023Article
- Straight to the point: targeted mRNA-delivery to immune cells for improved vaccine design.Frontiers in immunology · 2023Review
- Cell-targeted vaccines: implications for adaptive immunity.Frontiers in immunology · 2023Review
- Langerhans Cells-Revising Their Role in Skin Pathologies.Journal of personalized medicine · 2022Review
- Synthesis of glycopeptides and glycopeptide conjugates.Organic & biomolecular chemistry · 2022Review
- From structure to function - Ligand recognition by myeloid C-type lectin receptors.Computational and structural biotechnology journal · 2022Review
- Future considerations for the mRNA-lipid nanoparticle vaccine platform.Current opinion in virology · 2021Review
- Specific Protein Antigen Delivery to Human Langerhans Cells in Intact Skin.Frontiers in immunology · 2021Article
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Langerhans cells (LCs) are antigen-presenting cells that reside in the skin. They uniquely express high levels of the C-type lectin receptor Langerin (CD207), which is an attractive target for antigen delivery in immunotherapeutic vaccination strategies against cancer. We here assess a library of 20 synthetic, well-defined mannoside clusters, built up from one, two, and three of six monomannosides, dimannosides, or trimannosides, appended to an oligopeptide backbone, for binding with Langerin using surface plasmon resonance and flow cytometric quantification. It is found that Langerin binding affinity increases with increasing number of mannosides. Hexavalent presentation of the mannosides resulted in binding affinities ranging from 3 to 12 μM. Trivalent presentation of the dimannosides and trimannosides led to Langerin affinity in the same range. The model melanoma gp100 antigenic peptide was subsequently equipped with a hexavalent cluster of the dimannosides and trimannosides as targeting moieties. Surprisingly, although the bifunctional conjugates were taken up in LCs in a Langerin-dependent manner, limited antigen presentation to cytotoxic T cells was observed. These results indicate that targeting glycan moieties on immunotherapeutic vaccines should not only be validated for target binding, but also on the continued effects on biology, such as antigen presentation to both CD8
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