The Plant Viruses: Polyhedral Virions with Tripartite by R. I. B. Francki (auth.), R. I. B. Francki (eds.)

By R. I. B. Francki (auth.), R. I. B. Francki (eds.)

It has been recognized for a very long time that almost all of plant viruses include RNA and long ago decade and a part it's been learned that many have genomes which include 3 molecules of single-stranded RNA with optimistic polarity. between those are viruses belonging to 4 teams well-known by means of the foreign Committee for Virus Taxonomy: the Bromovirus and Cucumovirus teams whose genomes are encapsi­ dated in small icosahedral debris or the Ilarvirus and alfalfa mosaic virus teams with spheroidal or bacilliform debris. as well as their tripartite genomes, those viruses percentage a few different houses and it's been proposed that they need to might be be grouped in one virus relations for which the identify Tricornaviridae has been recommended, the tri indicating the tripartite nature of the genome, the co emphasizing the cooperation of the 3 genome elements required to start up an infection, and the rna indicating that the genome consists of RNA. Viruses of this "family" are much less uniform of their organic right­ ties. a couple of them are common, inflicting very harmful plant ailments. Viruses equivalent to these of cucumber mosaic and alfalfa mosaic have very huge host levels and are liable for critical crop losses in lots of components of the area. Others corresponding to prunus necrotic ringspot or prune dwarf viruses are extra limited of their host levels yet by no means­ theless infect very important perennial hosts similar to stone end result and decrease productiveness considerably.

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Extra info for The Plant Viruses: Polyhedral Virions with Tripartite Genomes

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Figure 8 shows the overall quaternary structure derived for the AMV particles. The VRU strain differs only slightly in amino acid sequence from that of AMV 425 (Fig. , 1979). Nevertheless, the VRU strain is also capable of forming the stacked lattice, reflecting the polymorphism of the assembled protein. The proposed hexagonal surface lattice possesses twofold symmetry axes andd quasi-three- and quasi-sixfold axes. Two types of dimer interactions are in evidence, one producing a flat face (a dihedral angle of 180° between trimers) while the other utilizes a dihedral angel of about 140°, similar to that observed between trimers of an icosahedron.

However, there is no serological relationship between AMV and TSV or CVV or CLRV and the tryptic peptide maps of TSV and AMV protein show no similarity (van Vloten-Doting, 1975). Capsid proteins from the Bromo- and Cucumovirus groups will not activate Ilarvirus RNA. Recently, Roosien and van Vloten-Doting (1983) reported a coat protein mutant of AMV that formed a range of spheroidal particles virtually indistinguishable from those of TSV. The size of the particles was correlated with the amount of RNA encapsidated.

The icosahedral symmetry axes are indicated by the appropriate symbols while the quasi-threefold relates protein monomers A, B, and C. Figure 2 illustrates the orientation of the icosahedral (2, 3, 5) and quasi-symmetry axes (Q2, Q3, Q6). The quasi-sixfold is exemplified by the B2C relationship and the quasi-twofold by ABs. , 1983a) are indicated by various patterns which, if identical, refer to similar subunit contacts. i i ~~ •. ~. 22 JOHN E. , T = 2 not permitted) allow equivalent and quasi-equivalent symmetry, itself required by use of identical protein subunits.

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