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Recognition of microbial glycans by human intelectin-1

Darryl A Wesener1, Kittikhun Wangkanont2, Ryan McBride3

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.

Nature Structural & Molecular Biology
|July 7, 2015
PubMed

Insights

Human intelectin-1 (hIntL-1) selectively binds microbial glycans, not human ones. This lectin

Area of Science:

  • Immunology
  • Glycobiology
  • Structural Biology

Background:

  • Mammalian and microbial cell surface glycans exhibit significant differences.
  • Carbohydrate-binding proteins (lectins) can potentially distinguish these glycan variations.

Purpose of the Study:

  • To investigate the glycan-binding specificity of human intelectin-1 (hIntL-1).
  • To elucidate the structural basis for hIntL-1's ligand recognition.

Main Methods:

  • Glycan microarray analysis to screen hIntL-1 binding.
  • X-ray crystallography to determine the structure of hIntL-1 in complex with a ligand.

Main Results:

  • hIntL-1 does not bind common human glycan epitopes.
  • hIntL-1 specifically interacts with microbial glycans, including β-linked D-galactofuranose (β-Galf), D-phosphoglycerol-modified glycans, heptoses, KDO, and KO.
  • Crystal structure reveals hIntL-1 utilizes a calcium ion to bind terminal 1,2-diols, explaining specificity against N-acetylneuraminic acid (Neu5Ac).
  • hIntL-1 recognizes specific *Streptococcus pneumoniae* serotypes expressing terminal 1,2-diol groups.

Conclusions:

  • hIntL-1 exhibits remarkable selectivity for microbial-specific glycan structures.
  • The findings suggest a role for hIntL-1 in microbial surveillance and host defense.

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