Language
English
Publication Date
5-5-2022
Journal
Communications Biology
DOI
10.1038/s42003-022-03357-1
PMID
35513489
PMCID
PMC9072675
PubMedCentral® Posted Date
5-5-2022
PubMedCentral® Full Text Version
Post-print
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.
Keywords
Capsid Proteins, Child, Crystallography, X-Ray, Galectins, Humans, Polysaccharides, Rotavirus, X-ray crystallography, Biochemistry
Published Open-Access
yes
Recommended Citation
Hu, Liya; Salmen, Wilhelm; Sankaran, Banumathi; et al., "Novel Fold of Rotavirus Glycan-Binding Domain Predicted by AlphaFold2 and Determined by X-Ray Crystallography" (2022). Faculty and Staff Publications. 3280.
https://digitalcommons.library.tmc.edu/baylor_docs/3280
Included in
Digestive System Diseases Commons, Gastroenterology Commons, Hepatology Commons, Medical Sciences Commons, Pediatrics Commons