Structural basis for the recognition of blood group trisaccharides by norovirus

被引:301
作者
Cao, Sheng
Lou, Zhiyong
Tan, Ming
Chen, Yutao
Liu, Yijin
Zhang, Zhushan
Zhang, Xuejun C.
Jiang, Xi
Li, Xuemei
Rao, Zihe
机构
[1] Univ Cincinnati, Coll Med, Cincinnati Childrens Hosp, Med Ctr,Div Infect Dis, Cincinnati, OH 45229 USA
[2] Chinese Acad Sci, Natl Lab Biomacrmol, Inst Biophys, Beijing 100101, Peoples R China
[3] Tsinghua Univ, Struct Biol Lab, Beijing 100084, Peoples R China
[4] Oklahoma Med Res Fdn, Crystallog Res Program, Oklahoma City, OK 73104 USA
关键词
D O I
10.1128/JVI.00219-07
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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-angstrom 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.
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页码:5949 / 5957
页数:9
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