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Irregular and Semi-Regular Polyhedral Models for Rous Sarcoma Virus Cores.

J Bernard Heymann1, Carmen Butan, Dennis C Winkler

  • 1Laboratory of Structural Biology Research, National Institute for Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda MD 20892;

Computational and Mathematical Methods in Medicine
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Retrovirus capsids, unlike those of many viruses, are polymorphic. New computational methods model these complex structures, revealing diverse shapes beyond simple icosahedral symmetry.

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Area of Science:

  • Structural virology
  • Biophysics
  • Computational biology

Background:

  • Many viruses possess highly symmetrical icosahedral capsids.
  • Retrovirus capsids are polymorphic and can be modeled as polyhedral structures based on fullerene lattices.
  • Determining retroviral capsid structure is challenging due to their lack of high symmetry.

Purpose of the Study:

  • To develop computational and graphical methods for constructing polyhedral models of retroviral capsids.
  • To analyze the shapes and symmetries of Rous sarcoma virus (RSV) capsids.
  • To understand the relationship between capsid shape and protein arrangement.

Main Methods:

  • Utilized cryo-electron tomography to observe RSV capsids within intact virions.
  • Developed computational and graphical methods to generate polyhedral models matching observed capsid size and shape.
  • Analyzed the distribution of pentamers and hexamers in capsid structures.

Main Results:

  • RSV capsids exhibit diverse shapes, including tubes, lozenges, and coffins.
  • Capsid shape variation correlates with the irregular distribution of the 12 essential pentamers.
  • The vast number of hexamers in RSV capsids (150-300) leads to millions of possible distinct polyhedral structures.
  • Retroviral capsid proteins display a continuum of conformations, unlike the limited conformations in icosahedral viruses.

Conclusions:

  • Computational modeling provides insights into the complex, non-icosahedral structures of retroviral capsids.
  • The polymorphism of retroviral capsids arises from the flexible arrangement of capsid proteins and their varied conformations.
  • These findings advance our understanding of retroviral assembly and evolution.