Structure of southern bean mosaic virus at 2.8 Å resolution

Abad‐Zapatero, Celerino; Abdel-Meguid, Sherin S.; Johnson, John E.; Leslie, Andrew G. W.; Rayment, Ivan; Rossmann, Michael G.; Suck, Dietrich; Tsukihara, Tomitake

doi:10.1038/286033a0

Cited by 381 publications

(156 citation statements)

References 40 publications

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“…These observations suggest the possibility of common features of polypeptide folding and subunit packing among rod-shaped plant viruses (Sawyer et al, 1987). Such common structural features have been revealed by three-dimensional structure determinations for the isometric plant viruses tomato bushy stunt (Harrison et al, 1978), southern bean mosaic (Abad-Zapatero et al, 1980) and satellite tobacco necrosis (Liljas et al, 1982) and the animal picornaviruses human rhinovirus 14 (Rossmann et al, 1985), poliovirus (Hogle et al, 1985) and Mengovirus (Luo et al, 1987) despite major differences in coat protein Mr (195 to 303 amino acids), amino acid sequence and, in the case of the animal picornaviruses, the presence of four rather than one type of coat protein. Thus, it would not be surprising if other rod-shaped plant viruses share structural features with the well studied tobacco mosaic virus particle.…”

mentioning

confidence: 73%

The N and C Termini of the Coat Proteins of Potyviruses Are Surface-located and the N Terminus Contains the Major Virus-specific Epitopes

Shukla

Strike

Tracy

et al. 1988

Journal of General Virology

281

241

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SUMMARYMild proteolysis by trypsin of particles of six potyviruses (bean yellow mosaic virus, clover yellow vein virus, Johnson grass mosaic virus, passion-fruit woodiness virus, potato virus Y and watermelon mosaic virus II) revealed that the N-and C-terminal regions of their coat protein are exposed on the particles' surfaces. The enzyme treatment removed the N-terminal region (30 to 67 amino acids long, depending on the virus) and 18 to 20 amino acids from the C terminus of the coat proteins, leaving a fully assembled virus particle composed of coat protein cores consisting of 216 or 218 amino acid residues. These core particles were indistinguishable from untreated native particles in an electron microscope and were still infectious. The core particles lacked the virus-specific surface epitopes that are recognized by the bulk of the polyclonal antibodies raised against the whole virus particles. Epitopes thought to be groupspecific were located in the trypsin-resistant core protein region. The implications of these findings are discussed in relation to the similar surface location of the N-and Cterminal regions of the coat protein of other rod-shaped plant viruses and the observed common structural features displayed by isometric plant and animal viruses.

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mentioning

confidence: 73%

The N and C Termini of the Coat Proteins of Potyviruses Are Surface-located and the N Terminus Contains the Major Virus-specific Epitopes

Shukla

Strike

Tracy

et al. 1988

Journal of General Virology

281

241

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“…Many plant viruses have very basic, rather variable, aminoterminal extensions to their capsid proteins. These basic regions are almost invariably 'disordered' (for example, tomato bushy stunt virus 42 , southern bean mosaic virus 43 and satellite tobacco necrosis virus 44 ), lacking a unique conformation. When there is no especially basic protein component in the capsid protein, there usually is a significant amount of polyamines to neutralize the nucleic acid 45 .…”

Section: Protein Structurementioning

confidence: 99%

Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications

McKenna

Xia

Willingmann

et al. 1992

Nature

Self Cite

217

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The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage ΦX174. The F protein forms a T = 1 capsid whose major folding motif is the eightstranded antiparallel β barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating spikes that enclose a hydrophilic channel containing some diffuse electron density. Each G protein is a tight β barrel with its strands running radially outwards and with a topology similar to that of the F protein. The 12 'pilot' H proteins per virion may be partially located in the putative ion channel. The small, basic J protein is associated with the DNA and is situated in an interior cleft of the F protein. Tentatively, there are three regions of partially ordered DNA structure, accounting for about 12% of the total genome.Bacteriophage ΦX174 is a small icosahedral virus that contains a single-stranded, closed circular DNA molecule with 5,386 nucleotide bases (for a recent review, see ref. 1). Of the 11 gene products, four (J, F, G and H) participate in the structure of the virion. There are 60 copies each of the J, F and G proteins and 12 copies of the H protein per virion [2][3][4] (Table 1). Electron microscopy of shadowed or negatively stained particles [5][6][7][8] , as well as a threedimensional reconstruction of frozen-hydrated virions (Fig. 1a), clearly show large spikes at the vertices of the icosahedral particles (N.H.O., T.S.B., P.W. and N.L.I., manuscript in preparation). These spikes are about 32 Å long and have a mean diameter of 70 Å. Edgell et al. 3 have shown that these spikes, which can be removed from the capsid with 4 M urea treatment, are composed of G and H proteins. Assuming all 12 spikes are identical, then each spike will contain five G and one H protein 2 . The capsid itself has an external diameter of roughly 260 Å, with a protein shell that is about 30 Å thick, and contains the F and J proteins as well as the single-stranded (ss) DNA. The phage recognizes a lipopolysaccharide (LPS) receptor on the outer cell membrane of Escherichia coli [8][9][10][11] . Host range mutants, which determine which strains of E. coli are infected by ΦX174, map into the F, G and H genes [12][13][14][15] The infectious virion has a relative molecular mass of 6.2 × 10 6 (M r 6,200K) (26% is DNA) 32 . Lysates of infected E. coli contain two components which can be separated by sedimentation through a sucrose gradient 32,33 . The fast band contains the infectious 114S particles whereas the slow band contains noninfectious, 70S particles 32,34,35 . The latter contains about 20% of the normal DNA content with all of the genome represented in the population of particles. Both types of particles can be crystallized into isomorphous monoclinic crystals with space group P2 1 , and cell dimensions a = 305.6, b = 360.8, c = 299.5 Å, β = 92.89° that diffract at least to 2.6-Å resolution 33 . The asymmetric unit of the crystal cell contains one complete particle. We report here the three-dimensional structure...

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“…The four body diagonals of the pseudo-cubic cell are tetrahedral within experimental error. These body diagonals of the pseudo-cubic cell are along the of several viruses (Harrison, Olson, Schutt, Winkler & Bricogne, 1978;Abad-Zapatero et al, 1980;Liljas et al, 1982;Rossmann et al, 1985;Hogle, Chow & Filman, 1985). The recent determination of the structures of human rhino virus (Rossmann et al, 1985), polio virus (Hogle et al, 1985), black beetle virus (J. E. Johnson, personal communication) and cowpea mosaic virus (J. E. Johnson, personal communication) have demonstrated the power of the technique of molecular replacement for ab initio phasing X-ray reflections from crystals of biological macromolecules consisting of several copies of identical structural units.…”

Section: Discussionmentioning

confidence: 99%

Symmetry of belladonna mottle virus: rotation function studies

Munshi¹,

Hiremath²,

Murthy³

et al. 1987

Acta Crystallogr Sect B

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Belladonna mottle virus, a spherical plant virus belonging to the tymovirus group, was crystallized by precipitation with polyethylene glycol 6000 in sodium citrate buffer (pH 5.6). The crystals belong to rhombohedral space group R3 (a-~ 300 ,~, a = 60 °) with one molecule in the unit cell, and diffract X-rays to 3.5/~ resolution. Owing to the special interaxial angle of-60°, the lattice can also be described in terms of a pseudo-face-centred cubic cell. The face-centring vectors of the pseudo cell form the cell edges of the rhombohedral cell. The three-dimensional X-ray diffraction data on these crystals were collected using screenless oscillation photography to a resolution of 6/~. 37 842 independent reflections with I/cr(I) >-2-0 were measured on 51 filn ^pairs. The cell parameters were refined to a = 295.4Aand a = 59.86 ° by a postrefinement procedure. A rotation function was calculated using data between 11 and 13/~ resolution. The function unambiguously reveals the particle icosahedral symmetry and orientation in the unit cell. The body diagonals of the pseudo-cubic cell are nearly tetrahedral. The icosahedral particle also has a set of tetrahedrally related threefold axes. The particle orientation is such that these two sets can be made coincident by a rotation of -180 ° about the rhombohedral [ 111] direction.

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Structure of southern bean mosaic virus at 2.8 Å resolution

Cited by 381 publications

References 40 publications

The N and C Termini of the Coat Proteins of Potyviruses Are Surface-located and the N Terminus Contains the Major Virus-specific Epitopes

The N and C Termini of the Coat Proteins of Potyviruses Are Surface-located and the N Terminus Contains the Major Virus-specific Epitopes

Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications

Symmetry of belladonna mottle virus: rotation function studies

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