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07:02
Quantifying Human Norovirus Virus-like Particles Binding to Commensal Bacteria Using Flow Cytometry
Published on: April 29, 2020
Structural basis for the receptor binding specificity of Norwalk virus
Weiming Bu1, Aygun Mamedova, Ming Tan
1Division of Developmental Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229, USA.
Journal of Virology
|April 4, 2008
Summary
Noroviruses bind to host histo-blood group antigens. Structural analysis reveals distinct binding mechanisms between Norwalk virus (GI-1) and VA387 (GII-4) strains, explaining differences in antigen recognition.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Noroviruses are major causes of acute gastroenteritis in humans.
- Norovirus attachment to host cells relies on specific interactions with histo-blood group antigens.
- Different norovirus strains exhibit distinct patterns of histo-blood group antigen recognition.
Purpose of the Study:
- To elucidate the structural basis for differential ligand recognition in noroviruses.
- To compare the binding modes of the prototypic Norwalk virus (NV; GI-1) and VA387 (GII-4) to A antigen.
- To investigate the role of specific amino acid residues in NV P domain-antigen interactions.
Main Methods:
- X-ray crystallography of the Norwalk virus (NV) P domain with and without A trisaccharide.
- Cocrystallization of the NV P domain with A trisaccharide at 2.3-Å resolution.
- Mutational analysis of key residues in the NV P domain for antigen binding.
Main Results:
- The A trisaccharide binds to the NV P domain via interactions with Ser377, Asp327, His329, and Ser380.
- This binding mode is distinct from that observed in the VA387 P-domain-A-trisaccharide complex.
- The alpha-GalNAc residue of A trisaccharide is deeply buried in the NV binding pocket, unlike the alpha-fucose in VA387 complexes.
Conclusions:
- The structural differences in the P domain binding pockets explain the distinct histo-blood group antigen recognition profiles of NV and VA387.
- The NV binding mode for A trisaccharide is sterically incompatible with the VA387 P domain structure.
- Specific residues in the NV P domain are critical for binding to native A antigen.
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