ArticleCommunications biology2022
Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Protein Structure Prediction Methods.Advances in experimental medicine and biology · 2026Review
- From CASP13 to the Nobel Prize: DeepMind's AlphaFold Journey in Revolutionizing Protein Structure Prediction and Beyond.Current protein & peptide science · 2026Review
- Multiple rotavirus species encode fusion-associated small transmembrane (FAST) proteins with cell type-specific activity.Journal of virology · 2025Article
- Distance-AF improves predicted protein structure models by AlphaFold2 with user-specified distance constraints.Communications biology · 2025Article
- AlphaFold two years on: Validation and impact.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A predicted model-aided reconstruction algorithm for X-ray free-electron laser single-particle imaging.IUCrJ · 2024Article
- Predictive Modeling of Proteins Encoded by a Plant Virus Sheds a New Light on Their Structure and Inherent Multifunctionality.Biomolecules · 2024Article
- AlphaFold2 in biomedical research: facilitating the development of diagnostic strategies for disease.Frontiers in molecular biosciences · 2024Review
- AlphaFold2 and its applications in the fields of biology and medicine.Signal transduction and targeted therapy · 2023Review
- Exploring AlphaFold2's Performance on Predicting Amino Acid Side-Chain Conformations and Its Utility in Crystal Structure Determination of B318L Protein.International journal of molecular sciences · 2023Article
- AlphaFold2 protein structure prediction: Implications for drug discovery.Current opinion in structural biology · 2023Review
- 14th International dsRNA Virus Symposium, Banff, Alberta, Canada, 10-14 October 2022.Virus research · 2023Article
- Toward the appropriate interpretation of Alphafold2.Frontiers in artificial intelligence · 2023Review
- Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The VP8* domain of spike protein VP4 in group A and C rotaviruses, which cause epidemic gastroenteritis in children, exhibits a conserved galectin-like fold for recognizing glycans during cell entry. In group B rotavirus, which causes significant diarrheal outbreaks in adults, the VP8* domain (VP8*B) surprisingly lacks sequence similarity with VP8* of group A or group C rotavirus. Here, by using the recently developed AlphaFold2 for ab initio structure prediction and validating the predicted model by determining a 1.3-Å crystal structure, we show that VP8*B exhibits a novel fold distinct from the galectin fold. This fold with a β-sheet clasping an α-helix represents a new fold for glycan recognition based on glycan array screening, which shows that VP8*B recognizes glycans containing N-acetyllactosamine moiety. Although uncommon, our study illustrates how evolution can incorporate structurally distinct folds with similar functionality in a homologous protein within the same virus genus.
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