2. Academic Validation
  3. Recognition of microbial glycans by human intelectin-1

Recognition of microbial glycans by human intelectin-1

  • Nat Struct Mol Biol. 2015 Aug;22(8):603-10. doi: 10.1038/nsmb.3053.
Darryl A Wesener 1,  Kittikhun Wangkanont 2,  Ryan McBride 3,  Xuezheng Song 4,  Matthew B Kraft 2,  Heather L Hodges 2,  Lucas C Zarling 1,  Rebecca A Splain 2,  David F Smith 4,  Richard D Cummings 4,  James C Paulson 3,  Katrina T Forest 5,  Laura L Kiessling 6
Affiliations

Affiliations

  • 1 Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.
  • 2 Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.
  • 3 1] Department of Cell and Molecular Biology, Scripps Research Institute, La Jolla, California, USA. [2] Department of Chemical Physiology, Scripps Research Institute, La Jolla, California, USA.
  • 4 1] Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, USA. [2] Glycomics Center, Emory University School of Medicine, Atlanta, Georgia, USA.
  • 5 Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin, USA.
  • 6 1] Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA. [2] Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.
PMID: 26148048 DOI: 10.1038/nsmb.3053
Abstract

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: β-linked D-galactofuranose (β-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-Å-resolution crystal structure of hIntL-1 complexed with β-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.

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