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

TY - JOUR

T1 - Surface stresses in complex viral capsids and non-quasiequivalent viral architectures

AU - Indelicato, Giuliana

AU - Cermelli, Paolo

AU - Twarock, Reidun

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PY - 2020/8/5

Y1 - 2020/8/5

N2 - 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.

AB - 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.

KW - shear stress in viral capsids

KW - Capsid structure

KW - PRD1-adenovirus lineage

U2 - 10.1098/rsif.2020.0455

DO - 10.1098/rsif.2020.0455

M3 - Article

SN - 1742-5689

VL - 17

JO - Journal of the Royal Society Interface

JF - Journal of the Royal Society Interface

IS - 169

M1 - 20200455

ER -