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Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus
10:49

Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus

Published on: January 28, 2019

Alternative intermolecular contacts underlie the rotavirus VP5* two- to three-fold rearrangement

Joshua D Yoder1, Philip R Dormitzer

  • 1Program in Virology, Laboratory of Molecular Medicine, Harvard Medical School, Children's Hospital, Boston, MA 02115, USA.

The EMBO Journal
|March 3, 2006
PubMed

Insights

Rotavirus spike protein VP5* antigen domain can form dimers and trimers. This structural flexibility is key to rotavirus entry into cells and suggests potential as a subunit vaccine.

Area of Science:

  • Virology
  • Structural Biology
  • Vaccine Development

Background:

  • Rotavirus, a cause of childhood gastroenteritis, utilizes its spike protein VP4 for cell entry.
  • VP4 is cleaved into VP5*, which mediates membrane penetration and undergoes structural reorganization during viral entry.

Purpose of the Study:

  • To investigate the structural properties of a globular domain of VP5* (VP5* antigen domain).
  • To explore its potential as a subunit vaccine component.

Main Methods:

  • X-ray crystallography was used to determine the structures of the VP5* antigen domain in its dimer and trimer forms.
  • The solubility and antigenicity of the expressed domain were assessed.

Main Results:

  • The VP5* antigen domain autonomously folds and can form either well-ordered dimers or trimers.
  • The dimer structure resembles the spike on intact virions, while the trimer mimics the folded-back spike during cell entry.
  • The domain contains neutralizing epitopes and is soluble, indicating suitability for vaccine development.

Conclusions:

  • The VP5* antigen domain's ability to switch between dimer and trimer states facilitates rotavirus membrane penetration.
  • This domain is a promising candidate for a rotavirus subunit vaccine due to its structural properties and antigenicity.

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