ArticleThe Journal of biological chemistry2017
Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 42 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
- Article
- Calcium Competitive Inhibition of Langerin by Thiazolopyrimidinones.Journal of medicinal chemistry · 2025Article
- Development of Anti-Inflammatory Agents Utilizing DC-SIGN Mediated IL-10 Secretion in Autoimmune and Immune-Mediated Disorders: Bridging Veterinary and Human Health.International journal of molecular sciences · 2025Review
- Article
- Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- The unique 3D arrangement of macrophage galactose lectin enablesPNAS nexus · 2023Article
- Identification of the Allosteric Binding Site for Thiazolopyrimidine on the C-Type Lectin Langerin.ACS chemical biology · 2022Article
- Vector and Host C-Type Lectin Receptor (CLR)-Fc Fusion Proteins as a Cross-Species Comparative Approach to Screen for CLR-Rift Valley Fever Virus Interactions.International journal of molecular sciences · 2022Article
- Impact of Glycan Linkage toACS infectious diseases · 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
- On-Chip Neo-Glycopeptide Synthesis for Multivalent Glycan Presentation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- C-Type Lectins in Veterinary Species: Recent Advancements and Applications.International journal of molecular sciences · 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 Liposomal Platform for Delivery of a Protein Antigen to Langerin-Expressing Cells.Biochemistry · 2019Article
- Langerhans Cells SensemBio · 2019Article
- Mammalian sugar-binding receptors: known functions and unexplored roles.The FEBS journal · 2019Review
- Microarray Strategies for Exploring Bacterial Surface Glycans and Their Interactions With Glycan-Binding Proteins.Frontiers in microbiology · 2019Review
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
Abstract
The recognition of pathogen surface polysaccharides by glycan-binding proteins is a cornerstone of innate host defense. Many members of the C-type lectin receptor family serve as pattern recognition receptors facilitating pathogen uptake, antigen processing, and immunomodulation. Despite the high evolutionary pressure in host-pathogen interactions, it is still widely assumed that genetic homology conveys similar specificities. Here, we investigate the ligand specificities of the human and murine forms of the myeloid C-type lectin receptor langerin for simple and complex ligands augmented by structural insight into murine langerin. Although the two homologs share the same three-dimensional structure and recognize simple ligands identically, a screening of more than 300 bacterial polysaccharides revealed highly diverging avidity and selectivity for larger and more complex glycans. Structural and evolutionary conservation analysis identified a highly variable surface adjacent to the canonic binding site, potentially forming a secondary site of interaction for large glycans.
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Identifiers
What OpenQuestion holds
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.