We summarize some aspects of electrostatic interactions in the context of viruses. A simplified but, within well defined limitations, reliable approach is used to derive expressions for electrostatic energies and the corresponding osmotic pressures in single-stranded RNA viruses and double-stranded DNA bacteriophages. The two types of viruses differ crucially in the spatial distribution of their genome charge which leads to essential differences in their free energies, depending on the capsid size and total charge in a quite different fashion. Differences in the free energies are trailed by the corresponding characteristics and variations in the osmotic pressure between the inside of the virus and the external bathing solution.

We investigate the influence of salt concentration, charge on viral proteins and the length of single-stranded RNA (ssRNA) molecule on the spontaneous assembly of viruses. Only the nonspecific interactions are assumed to guide the assembly, i.e., we exclude any chemical specificity that may lock the viral proteins and ssRNA in preferred configurations. We demonstrate that the electrostatic interactions screened by the salt in the solution impose strong limits on viral composition that can be achieved by spontaneous assembly. In particular, we show that viruses whose ssRNA carries more than twice the amount of charge that is located on the viral proteins, cannot be assembled spontaneously. We find that the spatial distribution of protein charge is important for the energetics of the assembly. We also show that the pressures that act on the viruses as a result of attractive protein-ssRNA electrostatic interactions are at least an order of magnitude smaller than is the case with bacteriophage viruses that contain double-stranded DNA molecule.

We examine the role of electrostatic interactions in the assembly of empty spherical viral capsids. The charges on the protein subunits that make the viral capsid mutually interact and are expected to yield electrostatic repulsion acting against the assembly of capsids. Thus, attractive protein-protein interactions of non-electrostatic origin must act to enable the capsid formation. We investigate whether the interplay of repulsive electrostatic and attractive interactions between the protein subunits can result in the formation of spherical viral capsids of a preferred radius. For this to be the case, we find that the attractive interactions must depend on the angle between the neighboring protein subunits (i.e. on the mean curvature of the viral capsid) so that a particular angle(s) is (are) preferred energywise. Our results for the electrostatic contributions to energetics of viral capsids nicely correlate with recent experimental determinations of the energetics of protein-protein contacts in Hepatitis B virus [P. Ceres and A. Zlotnick, Biochemistry 41, 11525 (2002).].

Minimal energy shapes of closed, elastic shells with 12 pentagonal disclinations introduced in otherwise hexagonally coordinated crystalline lattice are studied. The geometry and the total energy of shells are studied as a function of the elastic properties of the material they are made of. Particular emphasis is put on the buckling transition of the shells, that is, a strong preference of the shell shapes to "buckle out" in spatial regions close to the pentagonal disclinations for a certain range of the elastic parameters of the problem. The transition effectively increases the mean square aspherity of shapes, making them look more like an icosahedron rather than a sphere, which is a preferred shape prior to the onset of the transition. The properties of the buckling transition are studied in cases when (i) the total volume enclosed by the elastic shell has to be fixed and when (ii) there is an internal pressure acting on the shell. This may be related to the maturation process in nonenveloped dsDNA viruses, where the insertion of the genetic material in a preformed protein shell (viral coating) may effectively impose the fixed volume and/or pressure constraint. Several scenarios that may explain the experimentally observed feature of mature viruses being more aspherical (facetted) from their immature precursors are discussed, and predictions for the elastic properties of viral coatings are obtained on the basis of the presented studies.