Journal
COMMUNICATIONS BIOLOGY
Volume 5, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s42003-022-03357-1
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Funding
- NIH [AI36040, AI080656, P30 DK56338]
- Robert Welch Foundation [Q1279]
- Gulf Coast Consortia, on the Training Interdisciplinary Pharmacology Scientists (TIPS) Program [T32 GM120011]
- DOE Office of Science User Facility [DE-AC02-05CH11231]
- National Institutes of Health, National Institute of General Medical Sciences [P30 GM124169-01]
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The VP8*B structure of group B rotavirus displays a novel fold for glycan recognition distinct from the galectin fold seen in group A and C rotaviruses. This study demonstrates how evolution can incorporate structurally distinct folds with similar functionality 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. 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-angstrom crystal structure, we show that VP8*B exhibits a novel fold distinct from the galectin fold. This fold with a beta-sheet clasping an alpha-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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