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Related Experiment Videos

Structural studies on the empty capsids of Physalis mottle virus.

S S Krishna1, M Sastri, H S Savithri

  • 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560 012, India.

Journal of Molecular Biology
|April 5, 2001
PubMed
Summary

The empty capsid structure of Physalis mottle tymovirus reveals significant radial expansion and altered subunit interactions compared to the full virus particle. RNA encapsidation induces ordering of N-terminal arms and particle radius reduction.

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Area of Science:

  • Structural biology
  • Virology
  • Biochemistry

Background:

  • Physalis mottle virus (PMV) is a plant virus with an icosahedral capsid.
  • Understanding the structural differences between empty and RNA-containing capsids is crucial for viral assembly and function.

Purpose of the Study:

  • To determine the three-dimensional crystal structure of the empty Physalis mottle tymovirus capsid.
  • To compare the structure of the empty capsid with the native, RNA-containing virus to understand structural changes upon RNA encapsidation.

Main Methods:

  • X-ray crystallography at 3.2 A resolution.
  • Structure determination using real-space electron-density averaging with a known PMV structure as a phasing model.
  • Comparative analysis of empty and native capsid structures.

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Main Results:

  • The empty Physalis mottle tymovirus capsid structure was determined, revealing significant differences in N-terminal residues of subunits A, B, and C compared to the native virus.
  • Empty capsids showed a radial expansion of approximately 1.8 A, with altered subunit orientations relative to symmetry axes.
  • Pentamer-hexamer contacts were reduced in empty capsids, while the overall quaternary organization remained largely unchanged.

Conclusions:

  • RNA encapsidation in Physalis mottle virus leads to a reduction in particle radius and ordering of N-terminal arms.
  • The observed structural changes upon RNA encapsidation are more pronounced than in other studied viruses.
  • These findings provide insights into the dynamic structural rearrangements during viral assembly.