Structural highlights
Publication Abstract from PubMed
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.
The sweet quartet: Binding of fucose to the norovirus capsid.,Koromyslova AD, Leuthold MM, Bowler MW, Hansman GS Virology. 2015 May 13;483:203-208. doi: 10.1016/j.virol.2015.04.006. PMID:25980740[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Koromyslova AD, Leuthold MM, Bowler MW, Hansman GS. The sweet quartet: Binding of fucose to the norovirus capsid. Virology. 2015 May 13;483:203-208. doi: 10.1016/j.virol.2015.04.006. PMID:25980740 doi:http://dx.doi.org/10.1016/j.virol.2015.04.006
