Further studies on ultrastructure of plants infected withPetunia ringspot virus

Rubio-Huertos, M.

doi:10.1007/bf01666304

Cited by 13 publications

(9 citation statements)

References 14 publications

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“…3A,B), crystals of virus particles ( fig. 3D) and X bodies of convoluted membranes were found in cells infected with PRSV and were similar to those found by R ubio-H uertos [8]. The tubes were 60-80 nm in diameter and contained approximately 10 particles in their circumference.…”

Section: Nasturtium Ringspot Virussupporting

confidence: 67%

“…Optical diffraction patterns of longitudinal sections of tubes gave a lattice spacing of about 13.0 nm and suggested that the hexagonal arrangement of virus particles was tilted to give a primary helix with a pitch angle of about 20°. Optical diffraction patterns of crystals also showed a hexagonal arrangement with lattice spacing of about 13.0 nm; a similar lattice spacing was obtained from examination of the crystal shown in figure 9 of R ubio-H uertos [8], It is probable that this lattice spacing represents half the distance between centers of the particles [10].…”

Section: Nasturtium Ringspot Virusmentioning

confidence: 66%

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The <i>in vivo </i>Behavior osf Broad Bean Wilt Virus and Three of its Strains

Hull¹,

Plaskitt²

1973

Intervirology

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The particles of broad bean wilt virus and three of its strains aggregated in different ways in infected cells of Chenopodium amaranticolor, C.quinoa and Nicotiana clevelandii. Most aggregates were crystals, interlocking networks of partides and sheets of particles rolled into different tubular forms or lying between adjacent mitochondria. One strain induces the formation of tubules consisting of a membrane around a file of particles. These structures are discussed with regard to the current ideas on the relationships between the virus strains.

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Section: Nasturtium Ringspot Virussupporting

confidence: 67%

Section: Nasturtium Ringspot Virusmentioning

confidence: 66%

The <i>in vivo </i>Behavior osf Broad Bean Wilt Virus and Three of its Strains

Hull¹,

Plaskitt²

1973

Intervirology

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“…No structural changes of the ER were observed in N. benthamiana plants infected with AMV (Carette, unpublished). By electron microscopy, tonoplast-associated vesicles have been observed in AMV-infected leaf tissue, appearing before cytoplasmic virus particles could be detected (28,42; J. van Lent, personal communication). Similarly, the formation of tonoplast-associated vesicles protruding into the vacuole has been reported for cucumovirus-infected cells (19,28) and was occasionally seen in cells infected with the ilarvirus Tobacco streak virus (28).…”

Section: P1 and P2 Replication Proteins Interact In Vitro And In Vivomentioning

confidence: 99%

Alfalfa Mosaic Virus Replicase Proteins P1 and P2 Interact and Colocalize at the Vacuolar Membrane

Heijden

Carette

Reinhoud

et al. 2001

J Virol

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Replication of Alfalfa mosaic virus (AMV) RNAs depends on the virus-encoded proteins P1 and P2. P1contains methyltransferase-and helicase-like domains, and P2 contains a polymerase-like domain. Coimmunoprecipitation experiments revealed an interaction between in vitro translated-P1 and P2 and showed that these proteins are present together in fractions with RNA-dependent RNA polymerase activity. A deletion analysis in the yeast two-hybrid system showed that in P1 the C-terminal sequence of 509 amino acids with the helicase domain was necessary for the interaction. In P2, the sequence of the N-terminal 241 aa was required for the interaction. In infected protoplasts, P1 and P2 colocalized at a membrane structure that was identified as the tonoplast (i.e., the membrane that surrounds the vacuoles) by using a tonoplast intrinsic protein as a marker in immunofluorescence studies. While P1 was exclusively localized on the tonoplast, P2 was found both at the tonoplast and at other locations in the cell. As Brome mosaic virus replication complexes have been found to be associated with the endoplasmic reticulum (M. A. Restrepo-Hartwig and P. Ahlquist, J. Virol. 70:8908-8916, 1996), viruses in the family Bromoviridae apparently select different cellular membranes for the assembly of their replication complexes.The alphavirus-like superfamily comprises a large number of animal and plant viruses sharing the properties of a capped, positive-stranded RNA genome and homologies in their RNA replication proteins. Despite homologies between the guanylytransferase/methyltransferase-like (MT), helicase-like (HEL), and polymerase-like (POL) domains, they may be expressed as parts of a single protein or as separate entities distributed over two or three proteins. Little is known about the nature of the interactions between these polypeptides and the ratio in which they are present in the viral replication complex, although purified RNA-dependent RNA polymerases (RdRp) have been used extensively to study viral replication in vitro. We have studied the interactions between the replicase proteins of Alfalfa mosaic virus (AMV) and their in situ localization to gain insight in the assembly of the replication complex.AMV is the type species of the genus Alfamovirus. It belongs to the Bromoviridae family of plant viruses, all having a tripartite RNA genome of messenger-sense polarity. RNA 3 encodes the movement protein (MP) and, via a subgenomic mRNA 4, the coat protein (CP). RNAs 1 and 2 encode the P1 and P2 replicase proteins, respectively. The N terminus of P1 contains a domain with sequence homology to the domains involved in RNA capping of the alphavirus Semliki Forest virus (SFV) nsP1 protein and the more closely related Brome mosaic virus (BMV) 1a protein (1, 2, 41). The C-terminal end of P1 has homology to the alphavirus-like supergroup of HEL domains (17,22), including the SFV nsP2 protein, for which helicase activity was recently shown in vitro (16). The P2 protein contains a central domain with sequence motifs conserved among ma...

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“…Petunia ringspot virus is transmitted by aphids and is thought to be spherical (Rubio-Huertos, 1968). The viruses have extensive and similar host ranges (Schmelzer, 196o;Doel, I972;Taylor & Stubbs, 1972;Doel, I973) and appear to be serologically identical (Cook & Gibbs, 197I;Doel, I972;Frowd & Tomlinson, 1972;Murant & Goold, 1972;Doel, I973;Sahambi et al 1973).…”

Section: Introductionmentioning

confidence: 99%

“…BBWV and NRSV do not appear to be serologically related to numerous isometric plant viruses (Taylor et al 1968;Verhoyen & Autrique, 1968). Cells infected with BBWV, NRSV or PRSV contain similar types of inclusion bodies (Rubio-Huertos, 1968; Virus purification. Both inoculated and systemically infected leaves of Chenopodium quinoa were harvested 6 to 8 days after inoculation and homogeni7ed with an equal quantity (v/w) of 0"5 M-potassium phosphate buffer containing 25 % (w/v) sucrose and o.o I M-cysteine-HC1, pH 7"o.…”

Section: Introductionmentioning

confidence: 99%

Comparative Properties of Type, Nasturtium Ringspot and Petunia Ringspot Strains of Broad Bean Wilt Virus

Doel

1975

Journal of General Virology

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SUMMARYThe purification and characterization of the type, nasturtium ringspot and petunia ringspot strains of broad bean wilt virus are described. The use of sucrose throughout purification reduced losses due to aggregation of the virus particles. Electron microscopy of virus preparations revealed particles which were apparently hexagonal in outline and approx. 27 nm in diam. Each virus had three sedimenting components, top (T), middle (M) and bottom (B), indistinguishable from those of cowpea mosaic virus (CPMV) in co-sedimentation experiments. The sedimentation coefficients, s°0,w of PRSV were 56S (T), 95S(M) and II6S(B). The buoyant densities of M and B components of BBWV, NRSV and PRSV in CSC1+2.34 (w/v) Igepon T73 were approx. 1.4o and 1.44 g/ml respectively. B components of the viruses contained a single RNA species (RNA-1) of mol. wt. 2.0 _+ o.I × Io 6 and approximate molar percentage base ratio of 26 ~oo guanine, 30 ~ adenine, 17"5 cytosine and 26-5 ~ uracil. M components of the viruses contained a single RNA species (RNA-2), mol. wt. 1.5 to 1.6 x lO 6. The base ratios of RNA-I and RNA-2 of BBWV were very similar. Mixtures of RNA-I and RNA-2 (or M and B components) were more infective than the separate RNA species (or virus components). Mol. wt. of the formaldehyde-denatured RNA species of BBWV, NRSV and PRSV were very similar to those of CPMV. BBWV, NRSV and PRSV contained two species of polypeptide, mol. wt. 42 ooo and 26 ooo.These properties in conjunction with serological evidence indicate that the viruses are closely related strains. The similarity between some of the properties of BBWV, NRSV and PRSV and those of CPMV is discussed.

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Further studies on ultrastructure of plants infected withPetunia ringspot virus

Cited by 13 publications

References 14 publications

The <i>in vivo </i>Behavior osf Broad Bean Wilt Virus and Three of its Strains

The <i>in vivo </i>Behavior osf Broad Bean Wilt Virus and Three of its Strains

Alfalfa Mosaic Virus Replicase Proteins P1 and P2 Interact and Colocalize at the Vacuolar Membrane

Comparative Properties of Type, Nasturtium Ringspot and Petunia Ringspot Strains of Broad Bean Wilt Virus

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