Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistep-binding of l-fucose to norovirus particles

Glycobiology. 2017 Jan;27(1):80-86. doi: 10.1093/glycob/cww070. Epub 2016 Aug 3.


Recently, combined nuclear magnetic resonance (NMR), native mass spectrometry (MS) and X-ray crystallographic studies have demonstrated that binding of histo-blood group antigens (HBGAs) to norovirus capsid protein (P-dimers) is a cooperative process involving four binding pockets. Here, we show that binding to norovirus virus-like particles (VLPs) is even more complex. We performed saturation transfer difference (STD) NMR titration experiments with two representative genotypes of norovirus VLPs using l-fucose as a minimal HBGA. Compared to titrations with P-dimers, the corresponding binding isotherms reflect at least six distinct binding events.

Keywords: STD NMR titrations; cooperative binding; norovirus infection; protein-carbohydrate interaction; virus-like particles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blood Group Antigens / chemistry*
  • Blood Group Antigens / metabolism
  • Blood Group Antigens / ultrastructure
  • Capsid Proteins / chemistry*
  • Capsid Proteins / ultrastructure
  • Crystallography, X-Ray
  • Fucose / chemistry
  • Humans
  • Magnetic Resonance Spectroscopy
  • Norovirus / chemistry*
  • Norovirus / ultrastructure
  • Protein Binding
  • Virion / chemistry
  • Virion / ultrastructure


  • Blood Group Antigens
  • Capsid Proteins
  • Fucose