ArticleJournal of virology2006
High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 84 citations in OpenAlex.
- Genetic and antigenic diversity of rotavirus A in faeces from Danish pigs.Virus evolution · 2026Article
- Genomic Analysis of Rotavirus G8P[8] Strains Detected in the United States Through Active Surveillance, 2016-2017.Viruses · 2025Article
- The Evolution of Post-Vaccine G8P[4] Group a Rotavirus Strains in Rwanda; Notable Variance at the Neutralization Epitope Sites.Pathogens (Basel, Switzerland) · 2023Article
- Genomic epidemiology of the rotavirus G2P[4] strains in coastal Kenya pre- and post-rotavirus vaccine introduction, 2012-8.Virus evolution · 2023Article
- Genomic characterization of the rotavirus G3P[8] strain in vaccinated children, reveals possible reassortment events between human and animal strains in Manhiça District, Mozambique.Frontiers in microbiology · 2023Article
- Structural Basis of Glycan Recognition of Rotavirus.Frontiers in molecular biosciences · 2021Review
- Comparative genomic analysis of genogroup 1 and genogroup 2 rotaviruses circulating in seven US cities, 2014-2016.Virus evolution · 2021Article
- Whole genome and in-silico analyses of G1P[8] rotavirus strains from pre- and post-vaccination periods in Rwanda.Scientific reports · 2020Article
- Human Neonatal Rotavirus Vaccine (RV3-BB) Produces Vaccine Take Irrespective of Histo-Blood Group Antigen Status.The Journal of infectious diseases · 2020Article
- Recombinant Subunit Rotavirus Trivalent Vaccine Candidate: Physicochemical Comparisons and Stability Evaluations of Three Protein Antigens.Journal of pharmaceutical sciences · 2020Article
- The C Terminus of Rotavirus VP4 Protein Contains an Actin Binding Domain Which Requires Cooperation with the Coiled-Coil Domain for Actin Remodeling.Journal of virology · 2019Article
- Pregnancy Galectinology: Insights Into a Complex Network of Glycan Binding Proteins.Frontiers in immunology · 2019Review
- Glycan Binding Specificity and Mechanism of Human and Porcine P[6]/P[19] Rotavirus VP8*s.Journal of virology · 2018Article
- Glycan recognition in globally dominant human rotaviruses.Nature communications · 2018Article
- Resurgence of Rotavirus Genotype G12 in St. Louis During the 2014-2015 Rotavirus Season.Journal of the Pediatric Infectious Diseases Society · 2017Article
- Structural basis of glycan specificity of P[19] VP8*: Implications for rotavirus zoonosis and evolution.PLoS pathogens · 2017Article
- VP4- and VP7-specific antibodies mediate heterotypic immunity to rotavirus in humans.Science translational medicine · 2017Article
- Functional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens.Journal of virology · 2016Article
- Diversity in Rotavirus-Host Glycan Interactions: A "Sweet" Spectrum.Cellular and molecular gastroenterology and hepatology · 2016Review
- Emergence of Rotavirus G12P[8] in St. Louis During the 2012-2013 Rotavirus Season.Journal of the Pediatric Infectious Diseases Society · 2015Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
Abstract
The most intensively studied rotavirus strains initially attach to cells when the "heads" of their protruding spikes bind cell surface sialic acid. Rotavirus strains that cause disease in humans do not bind this ligand. The structure of the sialic acid binding head (the VP8* core) from the simian rotavirus strain RRV has been reported, and neutralization epitopes have been mapped onto its surface. We report here a 1.6-A resolution crystal structure of the equivalent domain from the sialic acid-independent rotavirus strain DS-1, which causes gastroenteritis in humans. Although the RRV and DS-1 VP8* cores differ functionally, they share the same galectin-like fold. Differences between the RRV and DS-1 VP8* cores in the region that corresponds to the RRV sialic acid binding site make it unlikely that DS-1 VP8* binds an alternative carbohydrate ligand in this location. In the crystals, a surface cleft on each DS-1 VP8* core binds N-terminal residues from a neighboring molecule. This cleft may function as a ligand binding site during rotavirus replication. We also report an escape mutant analysis, which allows the mapping of heterotypic neutralizing epitopes recognized by human monoclonal antibodies onto the surface of the VP8* core. The distribution of escape mutations on the DS-1 VP8* core indicates that neutralizing antibodies that recognize VP8* of human rotavirus strains may bind a conformation of the spike that differs from those observed to date.
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