ArticleJournal of virology2018
Human Group C Rotavirus VP8*s Recognize Type A Histo-Blood Group Antigens as Ligands.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- CLDN3 inhibits rotavirus attachment by targeting residue 74 of VP7.PLoS pathogens · 2026Article
- Analysis between ABO blood group and clinical outcomes in COVID-19 patients and the potential mediating role of ACE2.Frontiers in medicine · 2023Article
- Article
- Rotavirus C Replication in Porcine Intestinal Enteroids Reveals Roles for Cellular Cholesterol and Sialic Acids.Viruses · 2022Article
- Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography.Communications biology · 2022Article
- From examining the relationship between (corona)viral adhesins and galectins to glyco-perspectives.Biophysical journal · 2021Article
- The Potential Contribution of ABO, Lewis and Secretor Histo-Blood Group Carbohydrates in Infection byFrontiers in cellular and infection microbiology · 2021Article
- 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
- Occurrence of four waterborne viruses at five typical raw water resources in the Republic of Korea during August 2013 to February 2019.Journal of microbiology (Seoul, Korea) · 2020Article
- Fondness for sugars of enteric viruses confronts them with human glycans genetic diversity.Human genetics · 2020Review
- Metagenomic sequencing generates the whole genomes of porcine rotavirus A, C, and H from the United States.PloS one · 2020Article
- Virus recognition of glycan receptors.Current opinion in virology · 2019Review
- Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins.Frontiers in chemistry · 2019Review
- Expression of the Hepatitis C Virus core-NS3 Fusion Protein on the Surface of Bacterial Ghosts: Prospects for Vaccine Production.Avicenna journal of medical biotechnologyArticle
Corrections and comments
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Authors and funding
14 authors at 8 institutions in 3 countries.
Funding
Abstract
Group/species C rotaviruses (RVCs) have been identified as important pathogens of acute gastroenteritis (AGE) in children, family-based outbreaks, as well as animal infections. However, little is known regarding their host-specific interaction, infection, and pathogenesis. In this study, we performed serial studies to characterize the function and structural features of a human G4P[2] RVC VP8* that is responsible for the host receptor interaction. Glycan microarrays demonstrated that the human RVC VP8* recognizes type A histo-blood group antigens (HBGAs), which was confirmed by synthetic glycan-/saliva-based binding assays and hemagglutination of red blood cells, establishing a paradigm of RVC VP8*-glycan interactions. Furthermore, the high-resolution crystal structure of the human RVC VP8* was solved, showing a typical galectin-like structure consisting of two β-sheets but with significant differences from cogent proteins of group A rotaviruses (RVAs). The VP8* in complex with a type A trisaccharide displays a novel ligand binding site that consists of a particular set of amino acid residues of the C-D, G-H, and K-L loops. RVC VP8* interacts with type A HBGAs through a unique mechanism compared with that used by RVAs. Our findings shed light on the host-virus interaction and the coevolution of RVCs and will facilitate the development of specific antivirals and vaccines.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.