AI Article Synopsis

  • Noroviruses (NoVs) are the leading cause of acute gastroenteritis globally, with Histo-blood group antigens (HBGAs) playing a crucial role in their attachment and host susceptibility.
  • The study focused on the GII.6 NoV genotype, investigating its binding to various HBGAs and revealing that it primarily interacts with A, B, and O secretor saliva, while not binding to non-secretors.
  • Researchers determined the crystal structure of the GII.6 and its interaction with H disaccharides, identifying key residues essential for binding, highlighting implications for NoV research, epidemiology, and potential antiviral drug development.

Article Abstract

Noroviruses (NoVs) are the primary cause of acute gastroenteritis worldwide. Histo-blood group antigens (HBGAs) are receptors or attachment factors that affect the prevalence and host susceptibility of NoVs. GII.6 NoV is one of the predominant genotypes in humans, which recognizes the type ABO secretor of HBGAs. However, the structural basis of GII.6 NoV's interaction with HBGAs receptors remains elusive. In this study, we investigated the binding features of the GII.6 strain to HBGAs using saliva- and glycan-ELISA assays and characterized the molecular basis of the GII.6 virus that recognizes H disaccharide. We showed that the GII.6 ​P domain recognized some A and O secretor's saliva samples, most B secretor's saliva samples, and H disaccharide antigen, but did not bind non-secretors' saliva. Further, we determined the crystal structures of GII.6 and its complex with H disaccharides at 1.7 ​Å, revealing that the P domain of GII.6 shares the conventional binding interface and mode of GII HBGAs. Single residue mutations at the GII.6-H binding sites could inhibit the binding of GII.6 to HBGAs, demonstrating that the interaction residues were crucial in maintaining NoV-glycan integrity. Finally, structural and sequence analyses showed that the major residues of the GII.6-H interaction were conserved among NoVs in the GII genogroup. Taken together, our study characterized the functional and structural features of GII.6 that allow it to interact with HBGAs, and shed light on NoV evolution, epidemiology, and anti-viral drug development.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10006186PMC
http://dx.doi.org/10.1016/j.virs.2022.09.010DOI Listing

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