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Related Experiment Videos

Inside polyomavirus at 25-A resolution.

J P Griffith1, D L Griffith, I Rayment

  • 1Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254.

Nature
|February 13, 1992
PubMed
Summary
This summary is machine-generated.

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Polyomavirus capsids and virions crystallize identically. Electron density maps reveal VP2 and VP3 molecules within the capsid, potentially guiding its assembly on the nucleohistone core.

Area of Science:

  • Structural biology
  • Virology
  • Biochemistry

Background:

  • Polyomavirus capsids are icosahedral structures composed of VP1 pentamers.
  • The precise arrangement and internal components of polyomavirus virions remain incompletely understood.

Purpose of the Study:

  • To determine the internal structure of the polyomavirus virion using X-ray diffraction.
  • To identify the location and potential role of internal viral proteins (VP2 and VP3).

Main Methods:

  • Difference Fourier analysis of X-ray diffraction data at 25-Å resolution.
  • Crystallization of empty polyomavirus capsids and complete virions.
  • Analysis of self-assembly of purified recombinant VP1.

Main Results:

Related Experiment Videos

  • Isomorphous crystallization of empty capsids and complete virions.
  • Electron density map revealing 72 prongs extending from the core into VP1 pentamer cavities.
  • Identification of these prongs with VP2 and VP3 molecules.

Conclusions:

  • VP2 and VP3 molecules are located within the polyomavirus capsid, interacting with VP1 pentamers.
  • These internal proteins may play a role in guiding capsid assembly onto the nucleohistone core.
  • The core itself shows no regular order in the electron density map.