ArticleThe Journal of biological chemistry2013
Common polymorphisms in human langerin change specificity for glycan ligands.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 55 citations in OpenAlex.
- Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026Review
- Structural insights into glycan recognition by plant immune receptors: a comparative perspective with animal innate immune systems.The Plant journal : for cell and molecular biology · 2026Review
- Review
- Medicinal chemistry of the myeloid C-type lectin receptors Mincle, Langerin, and DC-SIGN.RSC medicinal chemistry · 2021Review
- Article
- Analysis and Interpretation of the Impact of Missense Variants in Cancer.International journal of molecular sciences · 2021Review
- Association of Maternal DNA Methylation and Offspring Birthweight.Reproductive sciences (Thousand Oaks, Calif.) · 2021Article
- Molecular Recognition in C-Type Lectins: The Cases of DC-SIGN, Langerin, MGL, and L-Sectin.Chembiochem : a European journal of chemical biology · 2020Review
- A Common Genetic Variation in Langerin (CD207) Compromises Cellular Uptake of Staphylococcus aureus.Journal of innate immunity · 2020Article
- C-Type Lectin Receptors in Host Defense Against Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2020Review
- A Specific, Glycomimetic Langerin Ligand for Human Langerhans Cell Targeting.ACS central science · 2019Article
- Mammalian sugar-binding receptors: known functions and unexplored roles.The FEBS journal · 2019Review
- AmpliSeq Screening of Genes Encoding the C-Type Lectin Receptors and Their Signaling Components Reveals a Common Variant inFrontiers in immunology · 2018Article
- Lectins: a primer for histochemists and cell biologists.Histochemistry and cell biology · 2017Review
- Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent.The Journal of biological chemistry · 2017Article
- What contributes to an effective mannose recognition domain?Beilstein journal of organic chemistry · 2017Review
- Sweet complementarity: the functional pairing of glycans with lectins.Cellular and molecular life sciences : CMLS · 2016Review
- Alteration of the langerin oligomerization state affects Birbeck granule formation.Biophysical journal · 2015Article
- Increased density of tolerogenic dendritic cells in the small bowel mucosa of celiac patients.World journal of gastroenterology · 2015Article
- A Peptide Mimetic of 5-Acetylneuraminic Acid-Galactose Binds with High Avidity to Siglecs and NKG2D.PloS one · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Langerin, a C-type lectin on Langerhans cells, mediates carbohydrate-dependent uptake of pathogens in the first step of antigen presentation to the adaptive immune system. Langerin binds a diverse range of carbohydrates including high mannose structures, fucosylated blood group antigens, and glycans with terminal 6-sulfated galactose. Mutagenesis and quantitative binding assays indicate that salt bridges between the sulfate group and two lysine residues compensate for the nonoptimal binding of galactose at the primary Ca(2+) site. A commonly occurring single nucleotide polymorphism (SNP) in human langerin results in change of one of these lysine residues, Lys-313, to isoleucine. Glycan array screening reveals that this amino acid change abolishes binding to oligosaccharides with terminal 6SO4-Gal and enhances binding to oligosaccharides with terminal GlcNAc residues. Structural analysis shows that enhanced binding to GlcNAc may result from Ile-313 packing against the N-acetyl group. The K313I polymorphism is tightly linked to another SNP that results in the change N288D, which reduces affinity for glycan ligands by destabilizing the Ca(2+)-binding site. Langerin with Asp-288 and Ile-313 shows no binding to 6SO4-Gal-terminated glycans and increased binding to GlcNAc-terminated structures, but overall decreased binding to glycans. Altered langerin function in individuals with the linked N288D and K313I polymorphisms may affect susceptibility to infection by microorganisms.
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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.