AChiralPentagonalPolyhedralFramework forCharacterizingVirusCapsidStructures

Trends Microbiol. 2017 Jun;25(6):438-446. doi: 10.1016/j.tim.2016.12.007. Epub 2017 Jan 13.

Abstract

Recent developments of rational strategies for the design of antiviral therapies, including monoclonal antibodies (mAbs), have naturally relied extensively on available viral structural information. As new strategies continue to be developed, it is equally important to continue to refine our understanding and interpretation of viral structural data. There are known limitations to the traditional (Caspar-Klug) theory for describing virus capsid structures that involves subdividing a capsid into triangular subunits. In this context, we describe a more general polyhedral framework for describing virus capsid structures that is able to account for many of these limitations, including a more thorough characterization of intersubunit interfaces. Additionally, our use of pentagonal subunits instead of triangular ones accounts for the intrinsic chirality observed in all capsids. In conjunction with the existing theory, the framework presented here provides a more complete picture of a capsid's structure and therefore can help contribute to the development of more effective antiviral strategies.

Keywords: pentagon; polyhedral; structure; virus.

Publication types

  • Review
  • Research Support, N.I.H., Extramural

MeSH terms

  • Capsid / chemistry*
  • Capsid / ultrastructure
  • Capsid Proteins / chemistry
  • Models, Biological
  • Protein Conformation*
  • Viral Structural Proteins / chemistry*
  • Viral Structural Proteins / ultrastructure
  • Virus Assembly

Substances

  • Capsid Proteins
  • Viral Structural Proteins