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Published on: April 19, 2016
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A Unique Human Norovirus Lineage with a Distinct HBGA Binding Interface
Wu Liu1, Yutao Chen2, Xi Jiang3
1School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, China.
Plos Pathogens
|July 7, 2015
Summary
Norovirus (NoV) evolution reveals a new lineage with a distinct histo-blood group antigen (HBGA) binding interface. This discovery, linked to glycerol
Area of Science:
- Virology
- Immunology
- Evolutionary Biology
Background:
- Norovirus (NoV) causes epidemic acute gastroenteritis.
- Histo-blood group antigens (HBGAs) are crucial for NoV host susceptibility.
- Major NoV genogroups (GI and GII) possess conserved HBGA binding interfaces.
Purpose of the Study:
- To characterize a novel Norovirus GII.21 strain (OIF virus) with a distinct HBGA binding profile.
- To investigate the evolutionary implications of this unique binding interface.
- To explore potential therapeutic strategies targeting NoV-HBGA interactions.
Main Methods:
- Characterization of the OIF virus strain.
- Sequence alignment of NoV strains.
- Analysis of HBGA binding interfaces.
- Inhibition assays using glycerol.
Main Results:
- Identified a GII.21 Norovirus strain (OIF virus) with a novel Lewis a (Lea) antigen binding interface.
- This interface deviates from the conserved GII binding pattern, indicating a new evolutionary lineage.
- Key residues for the novel binding interface are conserved in GII.21 and GII.13 genotypes.
- Glycerol was found to inhibit OIF virus binding to HBGAs.
Conclusions:
- A new evolutionary lineage of Norovirus, selected by HBGAs, has been identified.
- The distinct HBGA binding interface of the OIF virus expands our understanding of NoV diversity.
- Glycerol shows potential as a cost-effective antiviral agent against human Noroviruses.
