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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. © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.


Jonas Hanske, Jessica Schulze, Jonas Aretz, Ryan McBride, Bernhard Loll, Henrik Schmidt, Yuriy Knirel, Wolfgang Rabsch, Markus C Wahl, James C Paulson, Christoph Rademacher. Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent. The Journal of biological chemistry. 2017 Jan 20;292(3):862-871

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PMID: 27903635

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