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Updated: Apr 5, 2026

Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus
Published on: January 28, 2019
Substantial Receptor-induced Structural Rearrangement of Rotavirus VP8*: Potential Implications for Cross-Species
Xing Yu1, Rahul Mishra2, Gavan Holloway3
1Institute for Glycomics, Griffith University Gold Coast Campus, Southport, QLD, 4222, Australia. h.blanchard@griffith.edu.au.
Rotavirus VP8* protein undergoes significant structural changes when binding to host cell glycans. This adaptability explains how rotaviruses infect various hosts and aids in understanding animal rotavirus emergence in humans.
Area of Science:
- Virology
- Structural Biology
- Infectious Diseases
Background:
- Rotavirus infection initiates with host cell binding, a crucial step for tropism.
- The VP8* domain of the rotavirus VP4 spike protein mediates initial interactions via glycan receptors.
Purpose of the Study:
- To investigate the structural rearrangements of rotavirus VP8* upon glycan receptor binding.
- To understand the implications of VP8* structural adaptability for rotavirus host tropism and interspecies transmission.
Main Methods:
- Structural analysis of VP8* from human and animal rotavirus strains.
- Observation of VP8* structural changes following glycan receptor binding.
Main Results:
- First observation of significant structural rearrangement in rotavirus VP8* upon binding to glycan receptors.
- Demonstrated structural adaptability of VP8* across different rotavirus strains.
Conclusions:
- Rotavirus VP8* structural flexibility allows utilization of diverse cellular glycans.
- Findings provide insights into animal rotavirus gene emergence in humans and inform surveillance and vaccination strategies.
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