ArticlePLoS pathogens2017
Structural basis of glycan specificity of P[19] VP8*: Implications for rotavirus zoonosis and evolution.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 44 citations in OpenAlex.
- Whole-genome characterization and pathogenicity of novel human-porcine reassortant rotavirus strains G9P[7] and G1P[7] in China.Veterinary research · 2026Article
- Cross-neutralization and antigenic characterization of simian and equine group A rotaviruses.Journal of virology · 2026Article
- Factors contributing to the frequent interspecies transmission of G4P[6]Microbial genomics · 2026Article
- Precursor of H-type II histo-blood group antigen and subterminal sialic acids on gangliosides are significantly implicated in cell entry and infection by a porcine P[11] rotavirus.Emerging microbes & infections · 2025Article
- Driving forces of continuing evolution of rotaviruses.World journal of virology · 2024Review
- Review
- The αTSR Domain ofInternational journal of nanomedicine · 2023Article
- Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.Nature communications · 2022Article
- The Role of Host Glycobiology and Gut Microbiota in Rotavirus and Norovirus Infection, an Update.International journal of molecular sciences · 2021Review
- Glycan Recognition in Human Norovirus Infections.Viruses · 2021Review
- Noncovalent microarrays from synthetic amino-terminating glycans: Implications in expanding glycan microarray diversity and platform comparison.Glycobiology · 2021Article
- Structural basis of P[II] rotavirus evolution and host ranges under selection of histo-blood group antigens.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Rotavirus Vaccine Landscape, an Update.Pathogens (Basel, Switzerland) · 2021Review
- Mechanisms of Cell Entry by dsRNA Viruses: Insights for Efficient Delivery of dsRNA and Tools for Improved RNAi-Based Pest Control.Frontiers in physiology · 2021Review
- Infection of porcine small intestinal enteroids with human and pig rotavirus A strains reveals contrasting roles for histo-blood group antigens and terminal sialic acids.PLoS pathogens · 2021Article
- Structural Basis of Glycan Recognition of Rotavirus.Frontiers in molecular biosciences · 2021Review
- Rotavirus Interactions With Host Intestinal Epithelial Cells.Frontiers in immunology · 2021Review
- Histo-blood group antigens as divergent factors of groups A and C rotaviruses circulating in humans and different animal species.Emerging microbes & infections · 2020Article
- Rotavirus infection induces glycan availability to promote ileum-specific changes in the microbiome aiding rotavirus virulence.Gut microbes · 2020Article
- Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Recognition of specific cell surface glycans, mediated by the VP8* domain of the spike protein VP4, is the essential first step in rotavirus (RV) infection. Due to lack of direct structural information of virus-ligand interactions, the molecular basis of ligand-controlled host ranges of the major human RVs (P[8] and P[4]) in P[II] genogroup remains unknown. Here, through characterization of a minor P[II] RV (P[19]) that can infect both animals (pigs) and humans, we made an important advance to fill this knowledge gap by solving the crystal structures of the P[19] VP8* in complex with its ligands. Our data showed that P[19] RVs use a novel binding site that differs from the known ones of other genotypes/genogroups. This binding site is capable of interacting with two types of glycans, the mucin core and type 1 histo-blood group antigens (HBGAs) with a common GlcNAc as the central binding saccharide. The binding site is apparently shared by other P[II] RVs and possibly two genotypes (P[10] and P[12]) in P[I] as shown by their highly conserved GlcNAc-interacting residues. These data provide strong evidence of evolutionary connections among these human and animal RVs, pointing to a common ancestor in P[I] with a possible animal host origin. While the binding properties to GlcNAc-containing saccharides are maintained, changes in binding to additional residues, such as those in the polymorphic type 1 HBGAs may occur in the course of RV evolution, explaining the complex P[II] genogroup that mainly causes diseases in humans but also in some animals.
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