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Journal of Virology, June 2007, p. 5949-5957, Vol. 81, No. 11
0022-538X/07/$08.00+0     doi:10.1128/JVI.00219-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Structural Basis for the Recognition of Blood Group Trisaccharides by Norovirus{triangledown}

Sheng Cao,1,{dagger} Zhiyong Lou,2,{dagger} Ming Tan,3 Yutao Chen,1 Yijin Liu,1 Zhushan Zhang,1 Xuejun C. Zhang,1,4 Xi Jiang,3* Xuemei Li,1* and Zihe Rao1,2

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China,1 Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China,2 Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, University of Cincinnati College of Medicine, 3333 Burnet Avenue, Cincinnati, Ohio 45229-3039,3 Crystallography Research Program, Oklahoma Medical Research Foundation, 825 N.E. 13th Street, Oklahoma City, Oklahoma 731044

Received 31 January 2007/ Accepted 19 March 2007

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-Å 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.

* Corresponding author. Mailing address for Xi Jiang: Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, University of Cincinnati College of Medicine, 3333 Burnet Ave., Cincinnati, OH 45229-3039. Phone: (513) 636-0119. Fax: (513) 636-7655. E-mail: jason.jiang{at}cchmc.org. Mailing address for Xuemei Li: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China. Phone: 86-10-64888556. Fax: 86-10-64872026. E-mail: lixm{at}sun5.ibp.ac.cn

{triangledown} Published ahead of print on 28 March 2007.

{dagger} These authors contributed equally to this work.

Journal of Virology, June 2007, p. 5949-5957, Vol. 81, No. 11
0022-538X/07/$08.00+0     doi:10.1128/JVI.00219-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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