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Related Experiment Video

Updated: Jun 27, 2026

Subnanometer-Resolution Structural Determination of Hemagglutinin from Cryo-Electron Tomography of Influenza Viruses
08:19

Subnanometer-Resolution Structural Determination of Hemagglutinin from Cryo-Electron Tomography of Influenza Viruses

Published on: November 7, 2025

Rotavirus architecture at subnanometer resolution.

Zongli Li1, Matthew L Baker, Wen Jiang

  • 1National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA.

Journal of Virology
|November 28, 2008
PubMed
Summary
This summary is machine-generated.

This study presents a high-resolution structural model of rotavirus, detailing interactions between its major capsid proteins. The findings reveal the complex assembly of rotavirus, crucial for understanding infantile diarrhea.

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Sample Preparation for Single Virion Atomic Force Microscopy and Super-resolution Fluorescence Imaging
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Published on: January 2, 2014

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Subnanometer-Resolution Structural Determination of Hemagglutinin from Cryo-Electron Tomography of Influenza Viruses
08:19

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Published on: November 7, 2025

Sample Preparation for Single Virion Atomic Force Microscopy and Super-resolution Fluorescence Imaging
05:31

Sample Preparation for Single Virion Atomic Force Microscopy and Super-resolution Fluorescence Imaging

Published on: January 2, 2014

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Rotavirus causes severe infantile diarrhea and is a non-enveloped virus from the Reoviridae family.
  • Previous structural studies using X-ray crystallography and cryo-electron microscopy (cryoEM) provided partial structural information of rotavirus capsid proteins.

Purpose of the Study:

  • To develop a complete, high-resolution structural model of the infectious rotavirus particle.
  • To elucidate the intricate interactions among the major capsid proteins (VP2, VP4, VP6, VP7).

Main Methods:

  • Integration of advanced structural analysis techniques with subnanometer-resolution cryoEM data.
  • Detailed visualization and analysis of protein-protein interactions within the triple-layer capsid.

Main Results:

  • A high-resolution structural model of the complete rotavirus particle was generated.
  • Detailed interactions of the spike protein (VP4) as a dimer above the capsid and trimer at the base were identified.
  • Interactions between VP6 and VP7 subunits, and the VP2 inner layer with the VP6 layer were elucidated, revealing VP2's polypeptide fold.

Conclusions:

  • The study provides an unprecedented detailed structural model of infectious rotavirus.
  • Understanding these protein interactions offers insights into the assembly and stability of this large macromolecular complex.
  • This detailed model is crucial for future antiviral drug development and vaccine design against rotavirus infections.