A Unique Human Norovirus Lineage with a Distinct HBGA Binding Interface |
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| Authors: | Wu Liu Yutao Chen Xi Jiang Ming Xia Yang Yang Ming Tan Xuemei Li Zihe Rao |
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| Affiliation: | 1. School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, China.; 2. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.; 3. Division of Infectious Diseases, Cincinnati Children''s Hospital Medical Center, Cincinnati, Ohio United States of America.; 4. University of Cincinnati College of Medicine, Cincinnati, Ohio, United States of America.; University of Nantes INSERM, U892, FRANCE, |
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| Abstract: | Norovirus (NoV) causes epidemic acute gastroenteritis in humans, whereby histo-blood group antigens (HBGAs) play an important role in host susceptibility. Each of the two major genogroups (GI and GII) of human NoVs recognizes a unique set of HBGAs through a distinct binding interface that is conserved within a genogroup, indicating a distinct evolutionary path for each genogroup. Here, we characterize a Lewis a (Lea) antigen binding strain (OIF virus) in the GII.21 genotype that does not share the conserved GII binding interface, revealing a new evolution lineage with a distinct HBGA binding interface. Sequence alignment showed that the major residues contributing to the new HBGA binding interface are conserved among most members of the GII.21, as well as a closely related GII.13 genotype. In addition, we found that glycerol inhibits OIF binding to HBGAs, potentially allowing production of cheap antivirals against human NoVs. Taken together, our results reveal a new evolutionary lineage of NoVs selected by HBGAs, a finding that is important for understanding the diversity and widespread nature of NoVs. |
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