Key result
Covalently linking α-l-fucose to a lanthanide tag aids backbone NMR signal assignments of norovirus P-dimers.
Why the study?
Molecular details of human norovirus attachment to histo blood group antigens require backbone NMR signal assignments for study by protein NMR experiments.
Synthesis of a tagged α-l-fucose with a rigid lanthanide binding tag can aid in NMR backbone assignments of human norovirus coat proteins.
No immediate clinical implications; extends lanthanide tagging tools for norovirus NMR studies.
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.
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Mallagaray et al. (2015) studied Human norovirus infection (in vitro). α-l-fucose covalently linked to a rigid lanthanide binding tag was evaluated on Backbone NMR signal assignments. The synthesis of α-l-fucose covalently linked to a rigid lanthanide binding tag via a triazole linker was reported to aid backbone NMR signal assignments of human norovirus P-dimers.
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