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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Hauptverfasser: Koromyslova, Anna D. (VerfasserIn) , Leuthold, Mila (VerfasserIn) , Bowler, Matthew W. (VerfasserIn) , Hansman, Grant S. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 15 May 2015
In: Virology
Year: 2015, Jahrgang: 483, Pages: 203-208
ISSN:1096-0341
DOI:10.1016/j.virol.2015.04.006
Online-Zugang: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
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Verfasserangaben:Anna D. Koromyslova, Mila M. Leuthold, Matthew W. Bowler, Grant S. Hansman

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520 |a 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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