Tymoviruses

Hirth, L.; Givord, Louise

doi:10.1007/978-1-4613-0921-5_6

Cited by 22 publications

(19 citation statements)

References 192 publications

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“…Turnip yellow mosaic virus (TYMV), a T ¼ 3 icosahedral plant virus of 28 nm diameter, is one of the most thoroughly studied of all viruses [13][14][15][16][17]. The TYMV genome is made up of M r ¼ 1:9 Â 10 6 single-stranded RNA of 6218 bases [16], and a 694 nucleotide subgenomic RNA that is included in most virions.…”

Section: Methodsmentioning

confidence: 99%

“…The TYMV genome is made up of M r ¼ 1:9 Â 10 6 single-stranded RNA of 6218 bases [16], and a 694 nucleotide subgenomic RNA that is included in most virions. The structure of the virus was determined by X-ray diffraction analysis [18,19] from bipyramidal crystals (space group P6 4 22 with a ¼ b ¼ 515:0 ( A A and c ¼ 309:4 ( A A) grown from virus purified from Chinese cabbage by conventional procedures [13,18].…”

Section: Methodsmentioning

confidence: 99%

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Viral capsomere structure, surface processes and growth kinetics in the crystallization of macromolecular crystals visualized by in situ atomic force microscopy

Malkin

Kuznetsov

McPherson

2001

Journal of Crystal Growth

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Viral capsomere structure, surface processes and growth kinetics in the crystallization of macromolecular crystals visualized by in situ atomic force microscopy

Malkin

Kuznetsov

McPherson

2001

Journal of Crystal Growth

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“…1a, is one of the most thoroughly studied of all viruses (Markham and Smith, 1949;Matthews, 1991;Rubio-Huertos et al, 1967;Finch and Klug, 1966;Hirth and Givord, 1988;Mellema and Amos, 1972). The TYMV genome is made up of an M r ϭ 1.9 ϫ 10 6 , single-stranded RNA of 6218 bases (Hirth and Givord, 1988) and a 694-nucleotide subgenomic RNA that is included in most virions. The structure of the virus, shown in Fig.…”

Section: Methodsmentioning

confidence: 99%

Surface Processes in the Crystallization of Turnip Yellow Mosaic Virus Visualized by Atomic Force Microscopy

Malkin

Kuznetsov

Lucas

et al. 1999

Journal of Structural Biology

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In situ atomic force microscopy (AFM) was used to investigate surface evolution during the growth of single crystals of turnip yellow mosaic virus (TYMV). Growth of the (101) face of TYMV crystals proceeded by two-dimensional nucleation. The molecular structure of the step edges and adsorption of individual virus particles and their aggregates on the crystalline surface were recorded. The surfaces of individual virions within crystals were visualized and seen to be quite distinctive with the hexameric and pentameric capsomers of the T ‫؍‬ 3 capsids being clearly resolved. This, so far as we are aware, is the first direct visualization of the capsomere structure of a virus by AFM. In the course of recording the in situ development of the crystals, a profound restructuring of the surface arrangement was observed. This transformation was highly cooperative in nature, but the transitions were unambiguous and readily explicable in terms of an organized loss of classes of virus particles from specific lattice positions. In some cases areas of a single crystal surface were recorded in which were captured successive phases of the transition. We believe this provides the first visual record of a cooperative restructuring of the surface of a supramolecular crystal. 1999 Academic Press

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“…The CPs of icosahedral single-strand RNA bacteriophages, for which X-ray data have recently been reported (Valegaard et al, 1990), lack the jellyroll structure. The structures of the icosahedral capsids of tymoviruses and tricornaviruses have not been resolved, but there is evidence that their physicochemical properties are substantially different from those of the viruses with purported jellyroll domains (Hirth & Givord, 1988;Francki, 1985). Not surprisingly, the respective capsid proteins could not be included in the alignment shown in Fig.…”

Section: Search For Sequence Similarity In Other Capsid Proteinsmentioning

confidence: 99%

Phylogeny of capsid proteins of small icosahedral RNA plant viruses

Dolja

Koonin

1991

Journal of General Virology

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Statistically significant alignment was generated between the amino acid sequences of the (putative) shell (S) domains of the capsid proteins of small RNA plant viruses with icosahedral capsids in the tombusvirus, carmovirus, dianthovirus, sobemovirus and luteovirus groups. Inspection of the alignment showed good correspondence between the experimentally defined fl-strands and ~-helices of the capsid proteins of tomato bushy stunt, southern bean mosaic and turnip crinkle viruses, allowing prediction of the secondary structure elements in proteins with unresolved tertiary structure. It is concluded that this set of viral capsid proteins forms a tight evolutionary cluster. Comparison of the alignment of the proteins of this family with the sequences of other capsid proteins of icosahedral RNA viruses revealed more distant similarities to the satellites of tobacco necrosis, panicum mosaic, tobacco mosaic and maize white line mosaic viruses, as well as to nepo-and comoviruses. The tentative phylogenetic tree derived from the capsid protein alignment separated into three main lineages: (l) carmo-, tombus-and dianthoviruses, (II) southern bean mosaic, tobacco necrosis and maize chlorotic mottle viruses, and (III) luteoviruses. Comparison of this tree topology with the tentative evolutionary schemes for the respective virus RNA-dependent RNA polymerases suggested that gene shuffling is the universal trend in the evolution of small RNA plant virus genomes.

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Tymoviruses

Cited by 22 publications

References 192 publications

Viral capsomere structure, surface processes and growth kinetics in the crystallization of macromolecular crystals visualized by in situ atomic force microscopy

Viral capsomere structure, surface processes and growth kinetics in the crystallization of macromolecular crystals visualized by in situ atomic force microscopy

Surface Processes in the Crystallization of Turnip Yellow Mosaic Virus Visualized by Atomic Force Microscopy

Phylogeny of capsid proteins of small icosahedral RNA plant viruses

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