Structural analysis of bovine norovirus protruding domain
We determined a structure of a bovine (genogroup III, GIII) norovirus capsid protruding (P) domain using X-ray crystallography. The bovine P domain was reminiscent of other norovirus genogroups (GI, GII, GIV, and GV), but closely matched the human GI P domain. We also identified a monoclonal antibod...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
2016
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| In: |
Virology
Year: 2015, Volume: 487, Pages: 296-301 |
| ISSN: | 1096-0341 |
| DOI: | 10.1016/j.virol.2015.10.022 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.virol.2015.10.022 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S004268221500450X 
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| Author Notes: | Bishal Kumar Singh, Anna Koromyslova, Grant S. Hansman |
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| 520 | |a We determined a structure of a bovine (genogroup III, GIII) norovirus capsid protruding (P) domain using X-ray crystallography. The bovine P domain was reminiscent of other norovirus genogroups (GI, GII, GIV, and GV), but closely matched the human GI P domain. We also identified a monoclonal antibody that was capable of binding the five different (GI-GV) P domains. Our data suggests that genetically diverse noroviruses still contain common epitopes. | ||
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