Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 27903635Publication DOI: 10.1074/jbc.M116.751750Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: Christoph.Rademacher
mpikg.mpg.de
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany, Department of Biology, Chemistry, and Pharmacy, Freie Universitat Berlin, Berlin 14195, Germany, Department of Cell and Molecular Biology, Department of Immunology and Microbial Science and Department of Chemical Physiology, Scripps Research Institute, La Jolla, California 92037, Robert Koch Institute, Wernigerode Branch, National Reference Centre for Salmonellae and other Bacterial Enteric Pathogens, Wernigerode 38855, Germany
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.
polysaccharide, bacteria, Bacterial polysaccharide, lectin, innate immunity, animal model, langerin, C-type lectin, glycobiology, pattern recognition receptor (PRR)
Structure type: polymer chemical repeating unit
Location inside paper: p.867, fig.5A
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141807,IEDB_141830,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_152206,IEDB_983930,IEDB_983931,SB_136,SB_192,SB_196,SB_44,SB_67,SB_72
Methods: X-ray, SDS-PAGE, genetic methods, STD NMR, cloning, crystallization, ITC, glycan array analysis, flow cytometry analysis
3D data: 3D data
Related record ID(s): 11904, 11905, 12094, 12096, 12097, 12098, 12099
NCBI Taxonomy refs (TaxIDs): 2234096Reference(s) to other database(s): GTC:G73229TB
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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