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Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography.

Authors :
Hu L
Salmen W
Sankaran B
Lasanajak Y
Smith DF
Crawford SE
Estes MK
Prasad BVV
Source :
Communications biology [Commun Biol] 2022 May 05; Vol. 5 (1), pp. 419. Date of Electronic Publication: 2022 May 05.
Publication Year :
2022

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.<br /> (© 2022. The Author(s).)

Details

Language :
English
ISSN :
2399-3642
Volume :
5
Issue :
1
Database :
MEDLINE
Journal :
Communications biology
Publication Type :
Academic Journal
Accession number :
35513489
Full Text :
https://doi.org/10.1038/s42003-022-03357-1