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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

Sheng Cao,^1, Zhiyong Lou,^2, 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 Rao^1,2

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.

Published ahead of print on 28 March 2007.

These authors contributed equally to this work.

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