Structural analysis of a feline norovirus protruding domain
Norovirus infects different animals, including humans, mice, dogs, and cats. Here, we show an X-ray crystal structure of a feline GIV.2 norovirus capsid-protruding (P) domain to 2.35Å resolution. The feline GIV.2 P domain was reminiscent of human norovirus P domains, except for a novel P2 subdomain...
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| Main Authors: | , , , , , , |
|---|---|
| Format: | Article (Journal) |
| Language: | English |
| Published: |
2015
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| In: |
Virology
Year: 2014, Volume: 474, Pages: 181-185 |
| ISSN: | 1096-0341 |
| DOI: | 10.1016/j.virol.2014.10.028 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.virol.2014.10.028 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0042682214004851 
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| Author Notes: | Bishal K. Singh, Sebastian Glatt, Jean-Luc Ferrer, Anna D. Koromyslova, Mila M. Leuthold, Jessica Dunder, Grant S. Hansman |
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| 520 | |a Norovirus infects different animals, including humans, mice, dogs, and cats. Here, we show an X-ray crystal structure of a feline GIV.2 norovirus capsid-protruding (P) domain to 2.35Å resolution. The feline GIV.2 P domain was reminiscent of human norovirus P domains, except for a novel P2 subdomain α-helix and an extended P1 subdomain interface loop. These new structural features likely obstructed histo-blood group antigens, which are attachment factors for human norovirus, from binding at the equivalent sites on the feline GIV.2 P domain. Additionally, an ELISA showed that the feline GIV.2 was antigenically distinct from a human GII.10 norovirus. | ||
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