Open AccessStructural Basis for the Recognition of Blood Group Trisaccharides by Norovirus
Author(s) -
Sheng Cao,
Zhiyong Lou,
Ming Tan,
Yutao Chen,
Yijin Liu,
Zhushan Zhang,
Xuejun C. Zhang,
Xi Jiang,
Xuemei Li,
Zihe Rao
Publication year - 2007
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00219-07
Subject(s) - norovirus , biology , capsid , dimer , binding site , receptor , ligand (biochemistry) , plasma protein binding , virology , fucose , recombinant dna , neutralization , stereochemistry , glycoprotein , biochemistry , virus , chemistry , gene , organic chemistry
Noroviruses are one of the major causes of nonbacterial gastroenteritis epidemics in humans. Recent studies on norovirus receptors show that different noroviruses recognize different human histo-blood group antigens (HBGAs), and eight receptor binding patterns of noroviruses have been identified. The P domain of the norovirus capsids is directly involved in this recognition. To determine the precise locations and receptor binding modes of HBGA carbohydrates on the viral capsids, a recombinant P protein of a GII-4 strain norovirus, VA387, was cocrystallized with synthetic type A or B trisaccharides. Based on complex crystal structures observed at a 2.0-A resolution, we demonstrated that the receptor binding site lies at the outermost end of the P domain and forms an extensive hydrogen-bonding network with the saccharide ligand. The A and B trisaccharides display similar binding modes, and the common fucose ring plays a key role in this interaction. The extensive interface between the two protomers in a P dimer also plays a crucial role in the formation of the receptor binding interface.