Properties of turnip yellow mosaic virus in cesium chloride solutions: The formation of high-density components

Noort, A.; Dries, C.L.A.M. Van Den; Pleij, C.W.A.; Jaspars, E.M.J.; Bosch, L.

doi:10.1016/0042-6822(82)90041-1

Cited by 22 publications

(7 citation statements)

References 22 publications

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“…Variations of virion density detected in Cs' salt gradients indicate that many icosahedral capsids, including SBMV, would be permeable to Cs' (19)(20)(21). Our results show a channel sterically closed for Cs' (Fig.…”

Section: Discussionmentioning

confidence: 58%

“…In another two icosahedral plant virus whose structure has been determined, there are Thr residues around the fivefold axis towards the external viral capsid as Thr 126 and Thr 125 in SBMV. In tomato bushy stunt virus (TBSV) (21,23), Thr 170, Thr 171, and Trp 207 can be structurally superimposed to Thr 125, Thr 126, and Trp 162, respectively, in SBMV (24,25). That is, the channel entrance structure is similar in both virions even though the homology between amino acid sequences is only 20%.…”

Section: Discussionmentioning

confidence: 99%

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Ion Channels in Southern Bean Mosaic Virus Capsid

Silva¹,

Cachau²,

Goldstein³

1987

Biophysical Journal

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The study of southern bean mosaic virus protein coat high resolution model revealed a structure with properties of a natural protein-ion channel. Coat protein pentamers form a 30-A long channel and the amino acid composition of its wall bears some homology with the pentameric structure proposed for the nicotinic acetylcholine receptor channel. Ion transport properties were analyzed by computing ion-protein interaction energies on the basis of quantum chemistry methods. Energy maps show a channel attractive for cations, fully permeable to Li(+) and a narrow barrier for other cations and water. The energy profiles found are similar to the profiles determined for the K(+) channel of the sarcoplasmic reticulum. Comparisons with other icosahedral virus structures, including picornaviruses, suggest that ion channels would be a common feature of viral capsids. Biological roles for these channels are proposed.

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Section: Discussionmentioning

confidence: 58%

Section: Discussionmentioning

confidence: 99%

Ion Channels in Southern Bean Mosaic Virus Capsid

Silva¹,

Cachau²,

Goldstein³

1987

Biophysical Journal

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“…(1) high salt concentrations induce RNA aggregation, especially in the case of TYMV RNA (Pleij et al, 1976); (2) multivalent cations like Mg2+ and polyamines present in TYMV RNA samples are more firmly bound to the RNA at low ionic strength, thereby compensating for a low Na+ ion concentration in the buffer; (3) degradation of TYMV RNA appeared to be minimal at pH 6.0. The pattern obtained at higher RNA concentration points to the presence of one major RNA component (M, 2.0 X 106) which corresponds to the genome of TYMV (Noort et al, 1982). The asymmetry of the boundary suggests the presence of small amounts of faster sedimenting material that we ascribe to aggregated RNA.…”

Section: Resultsmentioning

confidence: 68%

Hydrodynamic properties of RNA: effect of multivalent cations on the sedimentation behavior of turnip yellow mosaic virus RNA

Eecen¹,

Dierendonck²,

Pleij³

et al. 1985

Biochemistry

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“…1C, fractions 9-12) contained the genomic RNA as well as residual amounts of sgRNAs of different sizes. Similarly, top-component particles of TYMV contained subgenomic CP mRNA, fragments of the genomic RNA, or host tRNAs (Noort et al, 1982;Szybiak et al, 1978).…”

Section: Cloning and Sequencing Of Pnmv Genomementioning

confidence: 99%

Sequence Analysis and Genome Organisation of Poinsettia Mosaic Virus (PnMV) Reveal Closer Relationship to Marafiviruses Than to Tymoviruses

2000

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Sequence comparison and genome organisation of poinsettia mosaic virus (PnMV), a putative member of the tymoviruses, revealed a closer relationship to marafiviruses. The complete nucleotide sequence of PnMV was determined. The 6099-nt RNA genome encodes a putative 221-kDa polyprotein that lacks a stop codon between the replicase and the coat protein genes, as in most tymovirus RNAs. The genomic RNA has a poly(A) tail at its 3Ј-terminus in contrast to the tRNA-like structure found in the RNA of most tymoviruses, and no homology was observed to the conserved noncoding region of the tymoviral 3Ј-termini. The tymobox of PnMV, a 16-nt region of the subgenomic RNA (sgRNA) promoter shared by most tymoviruses, differs in 3 nt from the RNA sequence of tymoviruses but is identical to the sequence of marafiviruses. At least three sgRNAs were found in PnMV-infected Euphorbia pulcherrima and in isolated PnMV particles; one that is 650 nt long encodes the 21.4-kDa coat protein, and the others are about 3.5 and 1.7 kb and contain the 5Ј-and the 3Ј-terminal parts of genomic RNA, respectively. Like tymoviruses, PnMV particles sediment as top and bottom components. The particles of the top component contain the sgRNA (650 nt) encoding the coat protein, and those of bottom component contain both genomic and sgRNAs.

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Properties of turnip yellow mosaic virus in cesium chloride solutions: The formation of high-density components

Cited by 22 publications

References 22 publications

Ion Channels in Southern Bean Mosaic Virus Capsid

Ion Channels in Southern Bean Mosaic Virus Capsid

Hydrodynamic properties of RNA: effect of multivalent cations on the sedimentation behavior of turnip yellow mosaic virus RNA

Sequence Analysis and Genome Organisation of Poinsettia Mosaic Virus (PnMV) Reveal Closer Relationship to Marafiviruses Than to Tymoviruses

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