title: Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent.
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.
authors.affiliation: From the Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany.|the Department of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, Berlin 14195, Germany.
authors.forename: Jonas
authors.initials: J
authors.lastname: Hanske
authors.affiliation: From the Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany.|the Department of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, Berlin 14195, Germany.
authors.forename: Jessica
authors.initials: J
authors.lastname: Schulze
authors.affiliation: From the Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany.|the Department of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, Berlin 14195, Germany.
authors.forename: Jonas
authors.initials: J
authors.lastname: Aretz
authors.affiliation: the Department of Cell and Molecular Biology, Department of Immunology and Microbial Science and Department of Chemical Physiology, Scripps Research Institute, La Jolla, California 92037.
authors.forename: Ryan
authors.initials: R
authors.lastname: McBride
authors.affiliation: the Department of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, Berlin 14195, Germany.
authors.forename: Bernhard
authors.initials: B
authors.lastname: Loll
authors.affiliation: From the Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany.|the Department of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, Berlin 14195, Germany.
authors.forename: Henrik
authors.initials: H
authors.lastname: Schmidt
authors.affiliation: the N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow 119991, Russia, and.
authors.forename: Yuriy
authors.initials: Y
authors.lastname: Knirel
authors.affiliation: the Robert Koch Institute, Wernigerode Branch, National Reference Centre for Salmonellae and other Bacterial Enteric Pathogens, Wernigerode 38855, Germany.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Rabsch
authors.affiliation: the Department of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, Berlin 14195, Germany.
authors.forename: Markus C
authors.initials: MC
authors.lastname: Wahl
authors.affiliation: the Department of Cell and Molecular Biology, Department of Immunology and Microbial Science and Department of Chemical Physiology, Scripps Research Institute, La Jolla, California 92037.
authors.forename: James C
authors.initials: JC
authors.lastname: Paulson
authors.affiliation: From the Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany, Christoph.Rademacher@mpikg.mpg.de.|the Department of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, Berlin 14195, Germany.
authors.forename: Christoph
authors.initials: C
authors.lastname: Rademacher
mesh_terms: D000818:Animals; D015703:Antigens, CD / Q000737:chemistry*; D000954:Antigens, Surface / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006801:Humans; D037181:Lectins, C-Type / Q000737:chemistry*; D037241:Mannose-Binding Lectins / Q000737:chemistry*; D051379:Mice; D011135:Polysaccharides, Bacterial / Q000737:chemistry*; D000072417:Protein Domains; D051192:Receptors, Pattern Recognition; D013045:Species Specificity
chemical_list: D015703:Antigens, CD; D000954:Antigens, Surface; C121916:CD207 protein, human; C498497:Cd207 protein, mouse; D037181:Lectins, C-Type; D037241:Mannose-Binding Lectins; D011135:Polysaccharides, Bacterial; D051192:Receptors, Pattern Recognition
keywords: C-type lectin; animal model; bacteria; glycobiology; innate immunity; langerin; lectin; pattern recognition receptor (PRR); polysaccharide