ArticleVirologica Sinica2020
Structural Basis of Glycan Recognition in Globally Predominant Human P[8] Rotavirus.
Article in Virologica Sinica, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Factors contributing to the frequent interspecies transmission of G4P[6]Microbial genomics · 2026Article
- The Impact of Methanol Concentration on Recombinant Protein Glycosylation in Pichia pastoris SuperMan5.Microbial biotechnology · 2025Article
- Specific binding of human P[28] rotavirus VP8* protein to blood group ABH antigens on type 1 chains.PLoS pathogens · 2025Article
- Culture of Human Rotaviruses in Relevant Models Shows Differences in Culture-Adapted and Nonculture-Adapted Strains.International journal of molecular sciences · 2023Article
- Differential transcriptome response following infection of porcine ileal enteroids with species A and C rotaviruses.Virology journal · 2023Article
- Milk lactose protects against porcine group A rotavirus infection.Frontiers in microbiology · 2022Article
- Glycan Recognition in Human Norovirus Infections.Viruses · 2021Review
- 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
- Genetic susceptibility to rotavirus infection in Chinese children: a population-based case-control study.Human vaccines & immunotherapeutics · 2021Article
- A Nanoparticle-Based Trivalent Vaccine Targeting the Glycan Binding VP8* Domains of Rotaviruses.Viruses · 2021Article
- Structural Basis of Glycan Recognition of Rotavirus.Frontiers in molecular biosciences · 2021Review
- Article
- Extracellular Vesicles in Human Preterm Colostrum Inhibit Infection by Human Cytomegalovirus In Vitro.Microorganisms · 2020Article
- Molecular basis of P[II] major human rotavirus VP8* domain recognition of histo-blood group antigens.PLoS pathogens · 2020Article
- Intestinal mucin-typeGut microbesReview
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotavirus (RV) causes acute gastroenteritis in infants and children worldwide. Recent studies showed that glycans such as histo-blood group antigens (HBGAs) function as cell attachment factors affecting RV host susceptibility and prevalence. P[8] is the predominant RV genotype in humans, but the structural basis of how P[8] RVs interact with glycan ligands remains elusive. In this study, we characterized the interactions between P[8] VP8*s and glycans which showed that VP8*, the RV glycan binding domain, recognized both mucin core 2 and H type 1 antigens according to the ELISA-based oligosaccharide binding assays. Importantly, we determined the structural basis of P[8] RV-glycans interaction from the crystal structures of a Rotateq P[8] VP8* in complex with core 2 and H type 1 glycans at 1.8 Å and 2.3 Å, respectively, revealing a common binding pocket and similar binding mode. Structural and sequence analysis demonstrated that the glycan binding site is conserved among RVs in the P[II] genogroup, while genotype-specific amino acid variations determined different glycan binding preference. Our data elucidated the detailed structural basis of the interactions between human P[8] RVs and different host glycan factors, shedding light on RV infection, epidemiology, and development of anti-viral agents.
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