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Updated: May 14, 2026

Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography
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Norwalk Virus Minor Capsid Protein VP2 Associates within the VP1 Shell Domain

Sompong Vongpunsawad1, B V Venkataram Prasad, Mary K Estes

  • 1Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA.

Journal of Virology
|February 15, 2013
PubMed

Insights

Norovirus VP1 protein forms the viral capsid. This study found that VP2 binds to the inner surface of VP1, specifically the S domain, which is crucial for VP2 incorporation into virus-like particles.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Norovirus VP1 protein self-assembles into an icosahedral capsid.
  • The minor structural protein VP2 is present in norovirus virions, but its location has remained elusive.
  • Understanding VP2's role is key to norovirus assembly and pathogenesis.

Purpose of the Study:

  • To determine the location and interaction site of norovirus VP2 within the viral capsid.
  • To elucidate the role of VP2 in norovirus assembly and genome encapsidation.

Main Methods:

  • Site-directed mutagenesis of the norovirus VP1 protein.
  • Analysis of virus-like particles (VLPs) using biochemical and structural techniques.
  • Mapping of protein-protein interaction interfaces.

Main Results:

  • Norovirus VP2 associates with the interior surface of the VP1 capsid, specifically with the S domain.
  • Amino acid 52 (isoleucine) within the conserved IDPWI motif in the VP1 S domain is critical for VP2 binding.
  • Mutation of this isoleucine residue prevents VP2 incorporation into VLPs without affecting VP1 assembly.
  • VP2's highly basic nature and internal location suggest a role in capsid assembly and genome packaging.

Conclusions:

  • VP2 binds to the inner surface of the norovirus capsid via a specific interaction with the VP1 S domain.
  • This interaction is essential for VP2 incorporation and likely plays a role in norovirus genome encapsidation.
  • The findings provide new insights into the structural organization and assembly mechanisms of noroviruses.

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