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Icosahedral Viruses (icosahedral + viruse)

Distribution by Scientific Domains
Chemistry100%

Selected Abstracts

Towards a classification of icosahedral viruses in terms of indexed polyhedra

ACTA CRYSTALLOGRAPHICA SECTION A, Issue 5 2006
A. Janner
The standard Caspar & Klug classification of icosahedral viruses by means of triangulation numbers and the more recent novel characterization of Twarock leading to a Penrose-like tessellation of the capsid of viruses not obeying the Caspar,Klug rules can be obtained as a special case in a new approach to the morphology of icosahedral viruses. Considered are polyhedra with icosahedral symmetry and rational indices. The law of rational indices, fundamental for crystals, implies vertices at points of a lattice (here icosahedral). In the present approach, in addition to the rotations of the icosahedral group 235, crystallographic scalings play an important rôle. Crystallographic means that the scalings leave the icosahedral lattice invariant or transform it to a sublattice (or to a superlattice). The combination of the rotations with these scalings (linear, planar and radial) permits edge, face and vertex decoration of the polyhedra. In the last case, satellite polyhedra are attached to the vertices of a central polyhedron, the whole being generated by the icosahedral group from a finite set of points with integer indices. Three viruses with a polyhedral enclosing form given by an icosahedron, a dodecahedron and a triacontahedron, respectively, are presented as illustration. Their cores share the same polyhedron as the capsid, both being in a crystallographic scaling relation. [source]

From structure of the complex to understanding of the biology

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 1 2007
Michael G. Rossmann
The most extensive structural information on viruses relates to apparently icosahedral virions and is based on X-ray crystallography and on cryo-electron microscopy (cryo-EM) single-particle reconstructions. Both techniques lean heavily on imposing icosahedral symmetry, thereby obscuring any deviation from the assumed symmetry. However, tailed bacteriophages have icosahedral or prolate icosahedral heads that have one obvious unique vertex where the genome can enter for DNA packaging and exit when infecting a host cell. The presence of the tail allows cryo-EM reconstructions in which the special vertex is used to orient the head in a unique manner. Some very large dsDNA icosahedral viruses also develop special vertices thought to be required for infecting host cells. Similarly, preliminary cryo-EM data for the small ssDNA canine parvovirus complexed with receptor suggests that these viruses, previously considered to be accurately icosahedral, might have some asymmetric properties that generate one preferred receptor-binding site on the viral surface. Comparisons are made between rhinoviruses that bind receptor molecules uniformly to all 60 equivalent binding sites, canine parvovirus, which appears to have a preferred receptor-binding site, and bacteriophage T4, which gains major biological advantages on account of its unique vertex and tail organelle. [source]

Structural analyses of Phycodnaviridae and Iridoviridae

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 12 2003
Alan A. Simpson
The Phycodnaviridae, Iridoviridae and related viruses, with diameters of 1500,2000,Ĺ, are formed from large trigonal arrays of hexagonally close-packed capsomers forming the faces of icosahedra [Yan et al. (2000), Nature Struct. Biol.7, 101,103; Nandhagopal et al. (2002), Proc. Natl Acad. Sci. USA, 99, 14758,14763]. Caspar and Klug predicted that such structures could be assembled from hexameric capsomers [Caspar & Klug (1962), Cold Spring Harbor. Symp. Quant. Biol.27, 1,24], as was subsequently found in numerous icosahedral viruses. During the course of evolution, some viruses, including the virus families mentioned above, replaced hexameric capsomers with pseudo-hexameric trimers by gene duplication. In large dsDNA icosahedral viruses, the capsomers are organized into `pentasymmetrons' and `trisymmetrons'. The interactions between the trimeric capsomers can be divided into three groups, one between similarly oriented trimers and two between oppositely oriented trimers (trimers related by an approximately sixfold rotation). The interactions within a trisymmetron belong to the first class, whereas those between trisymmetrons and within the pentasymmetron are of the other two types. Knowledge of these distances permits a more accurate fitting of the atomic structure of the capsomer into the cryo-electron microscopy (cryoEM) reconstruction of the whole virus. The adoption of pseudo-hexagonal capsomers places these viruses into a subset of the Caspar and Klug surface lattices. [source]