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

Autor: Hu L; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA. lhu@bcm.edu., Salmen W; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA., Sankaran B; Berkeley Center for Structural Biology, Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley Laboratory, Berkeley, CA, USA., Lasanajak Y; Emory Glycomics and Molecular Interactions Core (EGMIC), Emory University School of Medicine, Atlanta, GA, USA., Smith DF; Emory Glycomics and Molecular Interactions Core (EGMIC), Emory University School of Medicine, Atlanta, GA, USA., Crawford SE; Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX, USA., Estes MK; Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX, USA.; Department of Medicine, Baylor College of Medicine, Houston, TX, USA., Prasad BVV; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA. vprasad@bcm.edu.; Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX, USA. vprasad@bcm.edu.
Jazyk: angličtina
Zdroj: Communications biology [Commun Biol] 2022 May 05; Vol. 5 (1), pp. 419. Date of Electronic Publication: 2022 May 05.
DOI: 10.1038/s42003-022-03357-1
Abstrakt: 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.
(© 2022. The Author(s).)
Databáze: MEDLINE
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