A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus

Chem Commun (Camb). 2016 Jan 11;52(3):601-4. doi: 10.1039/c5cc05827a. Epub 2015 Nov 10.


Attachment of human noroviruses to histo blood group antigens is thought to be essential for infection of host cells. Molecular details of the attachment process can be studied in vitro using a variety of NMR experiments. The use of protein NMR based experiments requires assignments of backbone NMR signals. Using uniformly (2)H,(15)N-labeled protruding domains (P-dimers) of a prevalent epidemic human norovirus strain (GII.4 Saga) we have studied the potential of α-l-fucose covalently linked to a rigid lanthanide binding tag to aid backbone assignments using the paramagnetic properties of lanthanide ions. The synthesis of tagged α-l-fucose is reported. Notably, the metal chelating unit connects to the carbohydrate via a triazole linker constructed using click chemistry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blood Group Antigens / chemistry
  • Capsid Proteins / chemistry*
  • Dimerization
  • Fucose / chemistry
  • Humans
  • Lanthanoid Series Elements / chemistry*
  • Magnetic Resonance Spectroscopy
  • Norovirus / chemistry*
  • Protein Binding


  • Blood Group Antigens
  • Capsid Proteins
  • Lanthanoid Series Elements
  • Fucose