Structural rigidity in the capsid assembly of cowpea chlorotic mottle virus

B. M. Hespenheide, D. J. Jacobs, Michael Thorpe

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


The cowpea chlorotic mottle virus (CCMV) has a protein cage, or capsid, which encloses its genetic material. The structure of the capsid consists of 180 copies of a single protein that self-assemble inside a cell to form a complete capsid with icosahedral symmetry. The icosahedral surface can be naturally divided into pentagonal and hexagonal faces, and the formation of either of these faces has been proposed to be the first step in the capsid assembly process. We have used the software FIRST to analyse the rigidity of pentameric and hexameric substructures of the complete capsid to explore the viability of certain capsid assembly pathways. FIRST uses the 3D pebble game to determine structural rigidity, and a brief description of this algorithm, as applied to body-bar networks, is given here. We find that the pentameric substructure, which corresponds to a pentagonal face on the icosahedral surface, provides the best structural properties for nucleating the capsid assembly process, consistent with experimental observations.

Original languageEnglish (US)
Pages (from-to)S5055-S5064
JournalJournal of Physics Condensed Matter
Issue number44
StatePublished - Nov 10 2004

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics


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