7VS9
Crystal structure of P domain from norovirus GI.9 capsid protein in complex with Lewis x antigen.
Summary for 7VS9
| Entry DOI | 10.2210/pdb7vs9/pdb |
| Related PRD ID | PRD_900120 |
| Descriptor | VP1, alpha-L-fucopyranose-(1-3)-[beta-D-galactopyranose-(1-4)]2-acetamido-2-deoxy-alpha-D-glucopyranose, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | norovirus, p-domain, capsid, histo blood group antigen, viral protein |
| Biological source | Norovirus Hu/GI/Vancouver730/2004/CAN |
| Total number of polymer chains | 2 |
| Total formula weight | 69230.54 |
| Authors | Murayama, K.,Kato-Murayama, M.,Shirouzu, M. (deposition date: 2021-10-26, release date: 2022-08-31, Last modification date: 2023-11-29) |
| Primary citation | Kimura-Someya, T.,Kato-Murayama, M.,Katsura, K.,Sakai, N.,Murayama, K.,Hanada, K.,Shirouzu, M.,Someya, Y. Lewis fucose is a key moiety for the recognition of histo-blood group antigens by GI.9 norovirus, as revealed by structural analysis. Febs Open Bio, 12:560-570, 2022 Cited by PubMed Abstract: Noroviruses have been identified as major causative agents of acute nonbacterial gastroenteritis in humans. Histo-blood group antigens (HBGAs) are thought to play a major role among the host cellular factors influencing norovirus infection. Genogroup I, genotype 9 (GI.9) is the most recently identified genotype within genogroup I, whose representative strain is the Vancouver 730 norovirus. However, the molecular interactions between host antigens and the GI.9 capsid protein have not been investigated in detail. In this study, we demonstrate that the GI.9 norovirus preferentially binds Lewis antigens over blood group A, B, and H antigens, as revealed by an HBGA binding assay using virus-like particles. We determined the crystal structures of the protruding domain of the GI.9 capsid protein in the presence or absence of Lewis antigens. Our analysis demonstrated that Lewis fucose (α1-3/4 fucose) represents a key moiety for the GI.9 protein-HBGA interaction, thus suggesting that Lewis antigens might play a critical role during norovirus infection. In addition to previously reported findings, our observations may support the future design of antiviral agents and vaccines against noroviruses. PubMed: 35038379DOI: 10.1002/2211-5463.13370 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.26 Å) |
Structure validation
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