Surface stresses in complex viral capsids and non-quasi-equivalent viral architectures

• Published in: Journal of the Royal Society interface 2020-08, Vol.17 (169), p.20200455-20200455
• Main Authors: Indelicato, Giuliana, Cermelli, Paolo, Twarock, Reidun
• Format: Article
• Language: English
• Subjects: Capsid; Capsid Proteins; Life Sciences–Mathematics interface; Virion; Viruses
• ISSN: 1742-5689; 1742-5662
• DOI: 10.1098/rsif.2020.0455

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 (CP), they code for multiple distinct structural proteins that either break the local symmetry of the CP building blocks (capsomers) in specific positions or exhibit auxiliary proteins that stabilize 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 CPs, that represents the basic features of protein organization in the viral capsid as described in Caspar-Klug theory. We focus here on viruses in the PRD1-adenovirus lineage. For = 28 viruses in this lineage, which 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 = 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.