We propose the principles of structural organization in spherical nanoassemblies with icosahedral symmetry constituted by asymmetric protein molecules. The approach modifies the paradigmatic geometrical Caspar and Klug (CK) model of icosahedral viral capsids and demonstrates the common origin of both the "anomalous" and conventional capsid structures. In contrast to all previous models of "anomalous" viral capsids the proposed modified model conserves the basic structural principles of the CK approach and reveals the common hidden symmetry underlying all small viral shells. We demonstrate the common genesis of the "anomalous" and conventional capsids and explain their structures in the same frame. The organization principles are derived from the group theory analysis of the positional order on the spherical surface. The relationship between the modified CK geometrical model and the theory of two-dimensional spherical crystallization is discussed. We also apply the proposed approach to complex double-shelled capsids and capsids with protruding knob-like proteins. The introduced notion of commensurability for the concentric nanoshells explains the peculiarities of their organization and helps to predict analogous, but yet undiscovered, double-shelled viral capsid nanostructures.

We apply Landau theory of crystallization to explain and to classify the capsid structures of small viruses with spherical topology and icosahedral symmetry. We develop an explicit method which predicts the positions of centers of mass for the proteins constituting the viral capsid shell. Corresponding density distribution function which generates the positions has a universal form without any fitting parameter. The theory describes in a uniform way both the structures satisfying the well-known Caspar and Klug geometrical model for capsid construction and those violating it.

International audienceA new approach to the capsid structures of small viruses with spherical topology and icosahedral symmetry is proposed. It generalizes Landau theory of crystallization to describe icosahedral viral shells self-assembled from identical asymmetric proteins. An explicit method which predicts the positions of centers of mass for the proteins constituting the shell is discussed in detail. The method is based on irreducible density distribution function which generates the protein positions. The universal form of the density distribution function which contains no fitting parameter permits to classify the capsids structures of small viruses. The theory describes in a uniform way both the structures satisfying the well-known Caspar and Klug geometrical model for capsid construction and those violating it. A group theory analysis of the Caspar and Klug model and of the “quasiequivalence” principle for protein environments in viral capsids is given. The molecular basis of difference in protein environments and peculiarities in the assembly thermodynamics are also discussed