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Three-dimensional structure of calicivirus

B V Prasad1, D O Matson, A W Smith

  • 1Verna and Marrs Mclean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030.

Journal of Molecular Biology
|July 15, 1994
PubMed
Summary
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Researchers determined the 3D structure of a primate calicivirus, revealing unique T=3 icosahedral symmetry and arch-like capsomeres. This structural insight into caliciviruses aids understanding of viral assembly and evolution.

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Caliciviridae is a viral family comprising single-stranded RNA viruses.
  • Human caliciviruses are known to cause gastroenteritis.
  • Animal caliciviruses are associated with a diverse range of diseases.

Purpose of the Study:

  • To determine the three-dimensional structure of a primate calicivirus.
  • To elucidate the structural organization and symmetry of the calicivirus capsid.
  • To compare the structure of calicivirus with other known viral structures.

Main Methods:

  • Electron cryomicroscopy was employed to capture high-resolution images of the virus.
  • Computer image-processing techniques were utilized for 3D reconstruction.

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  • Analysis focused on the capsid's symmetry, protein subunits, and overall architecture.

    • Main Results:

    • The determined three-dimensional structure exhibits T=3 icosahedral symmetry and a diameter of 405 Å.
    • Key features include 32 large surface hollows and 90 arch-like capsomeres, each a dimer of the capsid protein.
    • Structural similarities were noted with certain plant viruses, despite distinct overall architecture from other animal viruses.

    Conclusions:

    • The calicivirus capsid is uniquely composed of a single structural protein.
    • Quasi-equivalent subunits display common structural domains (bilobed, stem, shell) with potential hinge regions.
    • The shell domain may feature a beta-barrel structure, with evidence of RNA interaction within the inner capsid.