Viruses icosahedral symmetry

The protein shells of spherical viruses have icosahedral symmetry... 

Any symmetric object is built up from smaller pieces that are identical and that are related to each other by symmetry. An icosahedron can therefore be divided into a number of smaller identical pieces called symmetry-related units. Protein subunits are asymmetric objects hence, a symmetry axis cannot pass through them. The minimum number of protein subunits that can form a virus shell with icosahedral symmetry is therefore equal to... 

The asymmetric unit of an icosahedron can contain one or several polypeptide chains. The protein shell of a spherical virus with icosahedral symmetry... 

Small spherical viruses have a protein shell around their nucleic acid that is constructed according to icosahedral symmetry. Objects with icosahedral symmetry have 60 identical units related by fivefold, threefold, and twofold symmetry axes. Each such unit can accommodate one or severed polypeptide chains. Hence, virus shells are built up from multiples of 60 polypeptide chains. To preserve quasi-equivalent symmetry when packing subunits into the shell, only certain multiples (T = 1, 3, 4, 7...) are allowed. 

The capsids of polyoma virus and the related SV40 have icosahedral symmetry, with 72 pentameric assemblies of the major capsid protein. The pentamers are linked to their neighbors by flexible arms, with a p strand that augments a p sheet in the invaded pentamer. These flexible arms allow the pentamers to be linked together with both fivefold and sixfold symmetry. 

Virus symmetry The nucleocapsids of viruses are constructed in highly symmetrical ways. Symmetry refers to the way in which the protein morphological units are arranged in the virus shell. When a symmetrical structure is rotated around an axis, the same form is seen again after a certain number of degrees of rotation. Two kinds of symmetry are recognized in viruses which correspond to the two primary shapes, rod and spherical. Rod-shaped viruses have helical symmetry and spherical viruses have icosahedral symmetry. 

One of the most intriguing recent examples of disordered structure is in tomato bushy stunt virus (Harrison et ah, 1978), where at least 33 N-terminal residues from subunit types A and B, and probably an additional 50 or 60 N-terminal residues from all three subunit types (as judged from the molecular weight), project into the central cavity of the virus particle and are completely invisible in the electron density map, as is the RNA inside. Neutron scattering (Chauvin et ah, 1978) shows an inner shell of protein separated from the main coat by a 30-A shell containing mainly RNA. The most likely presumption is that the N-terminal arms interact with the RNA, probably in a quite definite local conformation, but that they are flexibly hinged and can take up many different orientations relative to the 180 subunits forming the outer shell of the virus particle. The disorder of the arms is a necessary condition for their specific interaction with the RNA, which cannot pack with the icosahedral symmetry of the protein coat subunits. 

Electron microscopic studies have suggested that the alphavirus particle has icosahedral symmetry (see below). The triangulation number is not certain, however (Murphy, 1980). Previous estimates for the molecular weight were compatible with 240 subunits per virus particle, and electron micrographs appear to show a T = 4 surface lattice (von Bons-dorff and Harrison, 1975). More information is now needed to determine the surface organization, since compositional data show fewer than 240 subunits. 

Bluetongue virus, the prototype virus of the Orbivirus genus in the Reoviridae family, is an non-enveloped virus with seven structural proteins (VP1-VP7) [12]. The outer capsid consists of two proteins, VP2 and VPS. The core exhibits icosahedral symmetry and is composed of five proteins, two major (VPS and VP7) and three minor (VP1,VP4 and VP6) classified according to... 

Many virus coats have 180 subunits or a number that is some other multiple of 60. However, in these coats the subunits cannot all be in identical environments. Two cases may be distinguished. If all of the subunits have identical amino acid sequences they probably exist in more than one distinct conformation that permit them to pack efficiently. (Next section) Alternatively, two or more subunits of differing sequence and structure may associate to form 60 larger subunits that do pack with icosahedral symmetry. For example, the polioviruses (diameter 25 nm) contain three major coat proteins (a, P, and y or VP1, VP2, and VP3). These are formed by cleavage of a large precursor protein into at least four pieces.76 77 Tire three largest pieces of 33-, 30-, and 25-kDa mass (306,272, and 238 residues, respectively) aggregate as (aPy)60. Sixty copies of a fourth subunit of 60 residues are found within the shell. 

At the present time, there is no accepted chelating agent which can be used against common influenza viruses in humans. A virus has a core of either DNA or RNA and a protective coat of many identical protein units. All viruses are either rods or spheres, that is the protein coats are cylindrical shells having helical symmetry or spherical shells having icosahedral symmetry. Viruses reproduce inside living cells, where each viral nucleic acid directs the synthesis of about 1000 fresh viruses. These are then released and the host cell may die. 

CPMV particles have an icosahedral symmetry with a diameter of approximately 28 nm (Figure 9.2), the protein shell of the capsid is about 3.9nm thick [72], The structure of CPMV is known to near-atomic resolution (Figure 9.3) [73], The virions are formed by 60 copies of two different types of coat proteins, the small (S) subunit and the large (L) subunit. The S subunit (213 amino acids) folds into one jelly roll P-sandwich, and the L subunit (374 amino acids) folds into two jelly roll P-sandwich domains. The three domains form the asymmetric unit and are arranged in a similar surface lattice to T = 3 viruses, except they have different polypeptide sequences therefore the particle structure is described as a pseudo T = 3 or P = 3 symmetry [74]. 

Mackay called attention to yet another limitation of the 230 space-group system. It covers only those helices that are compatible with the three-dimensional lattices. All other helices that are finite in one or two dimensions are excluded. Some important virus structures with icosahedral symmetry are among them. Also, there are very small... 

Fig. 6. The Flock House virus has an icosahedral symmetry with the y-peptide and the C and N termini of the /3-protein lying internally and away from the surface. However, time resolved proteolysis data indicates that the viral capsid is highly mobile and that internal domains are transiently exposed on the surface...

Many of the ssRNA viruses have icosahedral symmetry. X-ray crystallographic structures of several of these viruses have been determined. In some of these structures, a significant portion of the genome is ordered. 

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