The sweet quartet: binding of fucose to the norovirus capsid
Human noroviruses bind histo-blood group antigens (HBGAs) and this interaction is thought to be important for an infection. We identified two additional fucose-binding pockets (termed fucose-3/4 sites) on a genogroup II human (GII.10) norovirus-protruding (P) dimer using X-ray crystallography. Fucos...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
15 May 2015
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| In: |
Virology
Year: 2015, Volume: 483, Pages: 203-208 |
| ISSN: | 1096-0341 |
| DOI: | 10.1016/j.virol.2015.04.006 |
| Online Access: | Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.virol.2015.04.006 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0042682215002032 |
| Author Notes: | Anna D. Koromyslova, Mila M. Leuthold, Matthew W. Bowler, Grant S. Hansman |
| Summary: | Human noroviruses bind histo-blood group antigens (HBGAs) and this interaction is thought to be important for an infection. We identified two additional fucose-binding pockets (termed fucose-3/4 sites) on a genogroup II human (GII.10) norovirus-protruding (P) dimer using X-ray crystallography. Fucose-3/4 sites were located between two previously determined HBGA binding pockets (termed fucose-1/2 sites). We found that four fucose molecules were capable of binding altogether at fucose-1/2/3/4 sites on the P dimer, though the fucose molecules bound in a dose-dependent and step-wise manner. We also showed that HBGA B-trisaccharide molecules bound in a similar way at the fucose-1/2 sites. Interestingly, we discovered that the monomers of the P dimer were asymmetrical in an unliganded state and when a single B-trisaccharide molecule bound, but were symmetrical when two B-trisaccharide molecules bound. We postulate that the symmetrical dimers might favor HBGA binding interactions at fucose-1/2 sites. |
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| Item Description: | Gesehen am 22.07.2020 |
| Physical Description: | Online Resource |
| ISSN: | 1096-0341 |
| DOI: | 10.1016/j.virol.2015.04.006 |