Surface stresses in complex viral capsids and non-quasiequivalent viral architectures

Research output: Contribution to journalArticlepeer-review


Many larger and more complex viruses deviate from the capsid layouts predicted in the seminal Caspar-Klug theory of icosahedral viruses. Instead of being built from one type of capsid protein, they code for multiple distinct structural proteins that either break the local symmetry of the capsid protein building blocks (capsomers) in specific positions, or exhibit auxiliary proteins that stabilise the capsid shell. We investigate here the hypothesis that this occurs as a response to mechanical stress. For this, we construct a coarse-grained model of a viral capsid, derived from the experimentally determined atomistic positions of the capsid proteins, that represents the basic features of protein organisation in the viral capsid as described in Caspar-Klug theory.
We focus here on viruses in the PRD1-adenovirus lineage. For T=28 viruses in this lineage, that have capsids formed from two distinct structural proteins, we show that the tangential shear stress in the viral capsid concentrates at the sites of local symmetry breaking. In the T=21,25 and 27 capsids, we show that stabilizing proteins decrease the tangential stress. These results suggest that mechanical properties can act as selective pressures on the evolution of capsid components, offsetting the coding cost imposed by the need for such additional protein components.
Original languageEnglish
Article number20200455
Number of pages15
JournalJournal of the Royal Society Interface
Issue number169
Publication statusPublished - 5 Aug 2020

Bibliographical note

This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.


  • shear stress in viral capsids
  • Capsid structure
  • PRD1-adenovirus lineage

Cite this