Identification of Beet Western Yellows Luteovirus Genes Implicated in Viral Replication and Particle Morphogenesis

Reutenauer, A.; Ziegler-Graff, Véronique; Lot, Hervé; Scheidecker, Danièle; Guilley, H.; Richards, K.; Jonard, G.

doi:10.1006/viro.1993.1420

Cited by 79 publications

(76 citation statements)

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“…The demonstration of RNA2-independent replication by RNA1 suggests that the presence of such a protein encoded by RNA2 is unnecessary. This result is also supported by recent mutagenesis studies, which demonstrated that the 19.5K protein encoded within the BWYV coat protein ORF was not essential for replication (Reutenauer et al, 1993). A second observation suggesting a possible replicative linkage between RNA1 and RNA2 involved the occurrence of conserved 40 nucleotide blocks preceding the coat protein ORF of RNA1 and the 26K and 27K protein-encoding ORFs of RNA 2.…”

Section: Discussionsupporting

confidence: 72%

Assessment of the Autonomy of Replicative and Structural Functions Encoded by the Luteo-phase of Pea Enation Mosaic Virus

Demler

Borkhsenious

Rucker

et al. 1994

Journal of General Virology

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The genome of pea enation mosaic virus (PEMV) is composed of two taxonomically unrelated RNAs, interacting to create what has traditionally been considered a bipartite virus. The cohesiveness of this interaction was assessed by examining the autonomy of each RNA in viral replication, coat protein expression and systemic invasion. Using a pea protoplast system, in vitro transcripts of RNA1 were found to be capable of initiating RNA2-independent replication, including the formation of the distinctive nuclear membrane-based replication complex associated with wild-type PEMV infection. Western blotting and electron microscopic analysis demonstrated that the synthesis of the RNA 1-encoded coat protein, as well as virion assembly, was also independent of RNA2-directed functions. Mechanical inoculations with transcripts of RNA 1 failed to establish a systemic RNA 1 infection, whereas inoculations with RNA2 were able to establish a largely asymptomatic systemic infection. Combined inoculum containing RNA1 and RNA2 transcripts were able to recreate wild-type PEMV symptomatology, demonstrating the dependence of RNA 1 on RNA2 for mechanical passage. With the notable exception of the adaptation of PEMV to establish a true systemic invasion, these data further strengthen the analogy between PEMV and the helper-dependent complexes associated with members of the luteovirus group.

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Section: Discussionsupporting

confidence: 72%

Assessment of the Autonomy of Replicative and Structural Functions Encoded by the Luteo-phase of Pea Enation Mosaic Virus

Demler

Borkhsenious

Rucker

et al. 1994

Journal of General Virology

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“…However, the latter is attached to the C terminus, rather than the N terminus, of P3 and there are no stretches of histidine residues or strongly acidic regions in the sequence of the readthrough protein. With BWYV, Reutenauer et al (1993) have shown that virus particles are formed in cells infected with mutants which, because of deletion, lack the readthrough protein.…”

Section: Discussionmentioning

confidence: 99%

Assembly of virus-like particles in insect cells infected with a baculovirus containing a modified coat protein gene of potato leafroll luteovirus

Lamb

Duncan²,

Reavy³

et al. 1996

Journal of General Virology

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DNA encoding the coat protein (P3) of a Scottish isolate of potato leafroll virus (PLRV) was inserted into the genome of Autographa californica nucleopolyhedrovirus (AcNPV) such that the coat protein was expressed either in an unmodified form or with the addition of the amino acid sequence MHHHH-HHGDDDDKDAMG at the N terminus (P3-6H). Insect cells infected with these recombinant baculoviruses accumulated substantial amounts of P3 and P3-6H. P3 could not be recovered from cell extracts unless it was denatured in SDS but a proportion of the P3-6H was recoverable in a soluble form in nondenaturing conditions. Immunogold labelling of sections of infected cells showed that P3 accumulated in nuclei in large amorphous bodies. In contrast, although much of the P3-6H also accumulated in nuclei, it formed virus-like particles (VLP) which were often grouped in close-packed, almost crystalline arrays. When electron microscope grids coated with antibodies to PLRV were floated on cell extracts containing P3-6H, VLP were trapped which were indistinguishable from PLRV particles trapped from extracts of PLRV-infected plants. The VLP cosedimented in sucrose gradients with PLRV particles which suggests that the VLP contained RNA. VLP collected from sucrose density gradient fractions contained protein which reacted with nickel chelated to nitrUotriacetic acid, a histidine-specific reagent. Cells infected with either recombinant baculovirus also synthesized a protein, with an M r of about 17000, which was shown to be the translation product of the P4 gene which is in the + 1 reading frame within the coat protein gene. This protein was also found in the nuclear fraction of infected cells but was more readily soluble than was P3.

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“…Consistent with a role in RNA replication, deletion mutations in ORFs 1 or 2 of PAV (77) or BWYV (86) destroyed the ability to replicate in plant cells.…”

Section: Replication Proteinsmentioning

confidence: 90%

“…In contrast to our speculation several years ago (76), ORF 4 does not encode a genome-linked protein (VPg). Despite much phylogenetic (70), biochemical (98), and genetic (77,86) evidence that ORF 4 does not encode the VPg, some researchers still refer to ORF 4 as encoding the VPg. Furthermore, we now have direct chemical evidence that PAV RNA lacks a VPg (E Allen, unpublished).…”

Section: Replication Proteinsmentioning

confidence: 99%

“…Besides its obvious function in forming virions, the coat protein (encoded by ORF 3) may have roles in virus movement in plants (119) and in replication. Mutations that render ORF 3 untranslatable reduced accumulation of genomic RNA of both BWYV (86) and PAV (77). This may be due to simple increased sensitivity of the genomic RNA to nucleases during extraction because it cannot be encapsidated, or the CP may be involved more directly in RNA replication.…”

Section: Structural Proteinsmentioning

confidence: 99%

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Barley Yellow Dwarf Viruses

Miller

Rasochova²

1997

Annu. Rev. Phytopathol.

215

154

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Barley yellow dwarf viruses represent one of the most economically important and ubiquitous groups of plant viruses. This review focuses primarily on four research areas in which progress has been most rapid. These include (a) evidence supporting reclassification of BYDVs into two genera; (b) elucidation of gene function and novel mechanisms controlling gene expression; (c) initial forays into understanding the complex interactions between BYDV virions and their aphid vectors; and (d ) replication of a BYDV satellite RNA. Economic losses, symptomatology, and means of control of BYD are also discussed.

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Identification of Beet Western Yellows Luteovirus Genes Implicated in Viral Replication and Particle Morphogenesis

Cited by 79 publications

References 0 publications

Assessment of the Autonomy of Replicative and Structural Functions Encoded by the Luteo-phase of Pea Enation Mosaic Virus

Assessment of the Autonomy of Replicative and Structural Functions Encoded by the Luteo-phase of Pea Enation Mosaic Virus

Assembly of virus-like particles in insect cells infected with a baculovirus containing a modified coat protein gene of potato leafroll luteovirus

Barley Yellow Dwarf Viruses

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