ArticlePloS one2012
Glycosaminoglycans are interactants of Langerin: comparison with gp120 highlights an unexpected calcium-independent binding mode.
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 18 papers.
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Who cites it
18 citing papers in PubMed, 47 citations in OpenAlex.
- Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026Review
- Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Multivalent, calcium-independent binding of surfactant protein A and D to sulfated glycosaminoglycans of the alveolar epithelial glycocalyx.American journal of physiology. Lung cellular and molecular physiology · 2024Article
- The unique 3D arrangement of macrophage galactose lectin enablesPNAS nexus · 2023Article
- Medicinal chemistry of the myeloid C-type lectin receptors Mincle, Langerin, and DC-SIGN.RSC medicinal chemistry · 2021Review
- DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist.PLoS pathogens · 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
- MASP-2 Is a Heparin-Binding Protease; Identification of Blocking Oligosaccharides.Frontiers in immunology · 2020Article
- A Specific, Glycomimetic Langerin Ligand for Human Langerhans Cell Targeting.ACS central science · 2019Article
- On-Chip Screening of a Glycomimetic Library with C-Type Lectins Reveals Structural Features Responsible for Preferential Binding of Dectin-2 over DC-SIGN/R and Langerin.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- Calcitonin Gene-Related Peptide Induces HIV-1 Proteasomal Degradation in Mucosal Langerhans Cells.Journal of virology · 2017Article
- Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent.The Journal of biological chemistry · 2017Article
- "Rules of Engagement" of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling.ChemistryOpen · 2016Review
- [Pulmonary Langerhans cell histiocytosis].Der Pathologe · 2015Review
- 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
- Recent advances in employing molecular modelling to determine the specificity of glycan-binding proteins.Current opinion in structural biology · 2014Review
- Common polymorphisms in human langerin change specificity for glycan ligands.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
8 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Langerin is a C-type lectin specifically expressed in Langerhans cells. As recently shown for HIV, Langerin is thought to capture pathogens and mediate their internalisation into Birbeck Granules for elimination. However, the precise functions of Langerin remain elusive, mostly because of the lack of information on its binding properties and physiological ligands. Based on recent reports that Langerin binds to sulfated sugars, we conducted here a comparative analysis of Langerin interaction with mannose-rich HIV glycoprotein gp120 and glycosaminoglycan (GAGs), a family of sulfated polysaccharides expressed at the surface of most mammalian cells. Our results first revealed that Langerin bound to these different glycans through very distinct mechanisms and led to the identification of a novel, GAG-specific binding mode within Langerin. In contrast to the canonical lectin domain, this new binding site showed no Ca(2+)-dependency, and could only be detected in entire, trimeric extracellular domains of Langerin. Interestingly binding to GAGs, did not simply rely on a net charge effect, but rather on more discrete saccharide features, such as 6-O-sulfation, or iduronic acid content. Using molecular modelling simulations, we proposed a model of Langerin/heparin complex, which located the GAG binding site at the interface of two of the three Carbohydrate-recognition domains of the protein, at the edge of the a-helix coiled-coil. To our knowledge, the binding properties that we have highlighted here for Langerin, have never been reported for C-type lectins before. These findings provide new insights towards the understanding of Langerin biological functions.
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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.