| First Author | Hanske J | Year | 2017 |
| Journal | J Biol Chem | Volume | 292 |
| Issue | 3 | Pages | 862-871 |
| PubMed ID | 27903635 | Mgi Jnum | J:239240 |
| Mgi Id | MGI:5828029 | Doi | 10.1074/jbc.M116.751750 |
| Citation | Hanske J, et al. (2017) Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent. J Biol Chem 292(3):862-871 |
| abstractText | 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. |
