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- Title
Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography.
- Authors
Hu, Liya; Salmen, Wilhelm; Sankaran, Banumathi; Lasanajak, Yi; Smith, David F.; Crawford, Sue E.; Estes, Mary K.; Prasad, B. V. Venkataram
- 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. Group B rotaviruses have a unique fold in the glycan-binding domain specific for N- acetyllactosamine that potentially diverged from folds conserved in group A and C rotaviruses.
- Subjects
ROTAVIRUSES; X-ray crystallography; CRYSTAL structure; PROTEIN domains; GLYCANS; GASTROENTERITIS; MOLECULAR recognition
- Publication
Communications Biology, 2022, Vol 5, Issue 1, p1
- ISSN
2399-3642
- Publication type
Article
- DOI
10.1038/s42003-022-03357-1