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The sweet quartet: Binding of fucose to the norovirus capsid.

Abstract：

: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.

journal_name

Virology

journal_title

Virology

authors

Koromyslova AD,Leuthold MM,Bowler MW,Hansman GS

doi

10.1016/j.virol.2015.04.006

subject

Has Abstract

pub_date

2015-09-01 00:00:00

pages

203-8

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(15)00203-2

journal_volume

483

pub_type

杂志文章

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