| First Author | Wesener DA | Year | 2015 |
| Journal | Nat Struct Mol Biol | Volume | 22 |
| Issue | 8 | Pages | 603-10 |
| PubMed ID | 26148048 | Mgi Jnum | J:237674 |
| Mgi Id | MGI:5816437 | Doi | 10.1038/nsmb.3053 |
| Citation | Wesener DA, et al. (2015) Recognition of microbial glycans by human intelectin-1. Nat Struct Mol Biol 22(8):603-10 |
| abstractText | The glycans displayed on mammalian cells can differ markedly from those on microbes. Such differences could, in principle, be 'read' by carbohydrate-binding proteins, or lectins. We used glycan microarrays to show that human intelectin-1 (hIntL-1) does not bind known human glycan epitopes but does interact with multiple glycan epitopes found exclusively on microbes: beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, heptoses, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO). The 1.6-A-resolution crystal structure of hIntL-1 complexed with beta-Galf revealed that hIntL-1 uses a bound calcium ion to coordinate terminal exocyclic 1,2-diols. N-acetylneuraminic acid (Neu5Ac), a sialic acid widespread in human glycans, has an exocyclic 1,2-diol but does not bind hIntL-1, probably owing to unfavorable steric and electronic effects. hIntL-1 marks only Streptococcus pneumoniae serotypes that display surface glycans with terminal 1,2-diol groups. This ligand selectivity suggests that hIntL-1 functions in microbial surveillance. |
