Related Experiment Video
Updated: Jun 7, 2026
12:38
Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
Published on: August 9, 2011
Three-dimensional visualization of the rotavirus hemagglutinin structure
A L Shaw1, R Rothnagel, D Chen
1Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030.
Cell
|August 27, 1993
Summary
Structural analysis of rotavirus reveals the VP4 protein
Area of Science:
- Virology
- Structural Biology
- Microbiology
Background:
- Rotavirus is a leading cause of severe diarrheal disease in infants and young children worldwide.
- Understanding rotavirus structure is crucial for developing effective antiviral strategies and vaccines.
Purpose of the Study:
- To determine the three-dimensional structures of native simian and reassortant rotaviruses.
- To elucidate the role of the VP4 protein in rotavirus assembly and infectivity.
Main Methods:
- Electron cryomicroscopy
- Computer image processing
- In vivo radiolabeling studies
Main Results:
- The hemagglutinin spike is confirmed as a dimer of VP4.
- A poorly infectious reassortant virus lacking VP4 spikes was generated.
- A novel VP4 domain interacting with VP6 was identified, suggesting VP4's role in assembly and maturation.
Conclusions:
- VP4 assembly precedes VP7 assembly during rotavirus maturation.
- VP4 likely plays a critical role in receptor recognition and viral budding.
