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  Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent

Hanske, J., Schulze, J., Aretz, J., McBride, R., Loll, B., Schmidt, H., et al. (2017). Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent. The Journal of Biological Chemistry, 292(3), 862-871. doi:10.1074/jbc.M116.751750.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-1776-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-A79A-F
Genre: Journal Article

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 Creators:
Hanske, Jonas1, Author              
Schulze, Jessica1, Author              
Aretz, Jonas1, Author              
McBride, Ryan, Author
Loll, Bernhard, Author
Schmidt, Henrik1, Author              
Knirel, Yuriy, Author
Rabsch, Wolfgang, Author
Wahl, Markus C., Author
Paulson, James C., Author
Rademacher, Christoph1, Author              
Affiliations:
1Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863300              

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 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 on murine Langerin. Whereas 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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 Dates: 2016-11-302017
 Publication Status: Published in print
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 Identifiers: DOI: 10.1074/jbc.M116.751750
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 292 (3) Sequence Number: - Start / End Page: 862 - 871 Identifier: ISSN: 0021-9258