Sequence polymorphism in the 5'NTR and in the P1 coding region of potato virus Y genomic RNA

Tordo, V. Marie Jeanne; Chachulska, A. M.; Fakhfakh, H.; Romancer, Marc Le; Robaglia, Christophe; Astier-Manifacier, Suzanne

doi:10.1099/0022-1317-76-4-939

Cited by 72 publications

(47 citation statements)

References 52 publications

(64 reference statements)

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“…The subsequent nucleotides were added by systematic searching (when moving from the bound adenosine in 5'-4 3' direction) of the most probable interactions of VPg surface positive charges with subsequent phosphate groups of the RNA. This procedure is justified by experimental evidence (9,31) showing that the 5' end of potyviral RNA is probably single-stranded. Therefore we excluded the possibility that RNA-protein interaction specificity results from the formation of the RNA loop structures.…”

Section: Methodsmentioning

confidence: 99%

“…Sequencing the potato virus Y, common strain (PVYO), we detected a part of the viral open reading frame covering the putative VPg cistron, which translates into a protein of molecular mass equal to 25 kDa. In a study of the sequences of phenotypically different PVY strains, the PVY variants were recently classified into three phylogenetic groups (9). Strikingly, the first 20 5'-proximal RNA bases, covering the fragment which could be implicated in interaction with VPg, seem to be fully conserved in representatives of all subgroups (9).…”

mentioning

confidence: 99%

“…In a study of the sequences of phenotypically different PVY strains, the PVY variants were recently classified into three phylogenetic groups (9). Strikingly, the first 20 5'-proximal RNA bases, covering the fragment which could be implicated in interaction with VPg, seem to be fully conserved in representatives of all subgroups (9). The distal 5' nontranslated region varies significantly between the strains.…”

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confidence: 99%

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Three-dimensional model of the potyviral genome-linked protein.

Płochocka

Welnicki

Zielenkiewicz

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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The full sequence of the genome-linked viral protein (VPg) cistron located in the central part of potato virus Y (common strain) genome has been identified. The VPg gene codes for a protein of 188 amino acids, with significant homology to other known potyviral VPg polypeptides. A three-dimensional model structure of VPg is proposed on the basis of similarity of hydrophobic-hydrophilic residue distribution to the sequence of malate dehydrogenase of known crystal structure. The 5'. end of the viral RNA can be fitted to interact with the protein through the exposed hydroxyl group of Tyr-64, in agreement with experimental data. The complex favors stereochemically the formation of a phosphodiester bond [5'-(04-tyrosylphospho) The genome-linked viral protein (VPg) covalently bound to a 5'-terminal nucleotide of the genome has been identified for several animal and plant viruses, with both DNA and RNA genomes (1). Among positive-sense RNA viruses five families-luteoviruses, picornaviruses, comoviruses, nepoviruses, and potyviruses-are known to contain 5'-terminal VPg (1).The latter four families also share other similarities in RNA structure [3'-terminal poly(A) tail], genome organization (the presence of a characteristic cluster of replication genes), and strategy of expression (expression of viral RNA as a single polyprotein undergoing self-processing), and they are therefore often arranged in a supergroup of picornavirus-like viruses (2). In the potyvirus family, the area of our interest, genomic RNAs carry at their 5' end a VPg of molecular mass 22-24 kDa (3-5). As in polioviruses (6, 7), potyviral VPg binds to the 5'-phosphate through the hydroxyl group of a tyrosine (8). Sequencing the potato virus Y, common strain (PVYO), we detected a part of the viral open reading frame covering the putative VPg cistron, which translates into a protein of molecular mass equal to 25 kDa. In a study of the sequences of phenotypically different PVY strains, the PVY variants were recently classified into three phylogenetic groups (9). Strikingly, the first 20 5'-proximal RNA bases, covering the fragment which could be implicated in interaction with VPg, seem to be fully conserved in representatives of all subgroups (9). The distal 5' nontranslated region varies significantly between the strains. The conservation of the 5' terminus and of tyrosine implicated in RNA binding (8) suggests that constraints are imposed on their interaction.It can be inferred from the data on poliovirus (10, 11) that VPg binding to RNA is intimately related to the synthesis of progeny plus and minus RNA strands. It is suggested that a covalent [5'-(04-tyrosylphospho)adenylate] bond could be formed during potyviral RNA replication either by transesterification with nascent RNA chain or as a result of adenylylation of specific VPg tyrosine. Such VPg mono-(or oligo)adenylate could prime the progeny RNA synthesis. The two mechanisms are believed not to be mutually exclusive and could reflect the role of VPg in differentiation of viral plus and minus ...

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Three-dimensional model of the potyviral genome-linked protein.

Płochocka

Welnicki

Zielenkiewicz

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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“…The LYE84 isolate of PVY was a kind gift from K. G~br& S61assi6 (INRA, Avignon, France) and has been partially characterized (Tordo et al, 1995). It was propagated in Nicotiana tabacum var.…”

Section: Methodsmentioning

confidence: 99%

Nucleic acid-binding properties of a bacterially expressed potato virus Y helper component-proteinase

Maia

Bernardi

1996

Journal of General Virology

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The potyvirus helper component-proteinase (HC-Pro) is a multifunctional protein previously reported to have affinity for polyribonucleotides. To investigate further the ability of HC-Pro to bind nucleic acids, the potato virus Y (PVY) LYE84 isolate HC-Pro gene was amplified, cloned in an Escherichia coli expression vector and sequenced. HC-Pro was expressed as a fusion with the maltose-binding protein and purified by affinity chromatography. Electrophoretic mobility-shift assays demonstrated that HC-Pro acts as a sequence nonspecific RNA-binding protein and suggest that more than one molecule of protein was bound per molecule of RNA. The HC-Pro RNA-binding activity was stable in 400 mu-NaC1 and temperature sensitive. The recombinant protein preferentially bound ssRNA over DNA or dsRNA and showed little, if any, affinity for poly(A). The possible implications of the RNA-binding activity of HC-Pro in potyvirus replication and movement are discussed.

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“…andigena), leading to the development of internal and external necrotic symptoms on the progeny tubers, which reflects the necrogenic reaction of hypersensitivity (Le Romancer & Kerlan, 1992;Le Romancer, 1993). They also differ in their nucleotide sequence (Marie Jeanne Tordo et al, 1995) and probably originate from genomic recombination events (Revers et al, 1996), leading to the new subgroup currently referred to as PVY NTN .…”

Section: Introductionmentioning

confidence: 99%

Effect of plant genotype, virus isolate and temperature on the expression of the potato tuber necrotic ringspot disease (PTNRD)

Romancer

Nedellec²

1997

Plant Pathology

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The present study shows that a large range of potato cultivars (29/33 tested), widely grown in the world, are susceptible to potato tuber necrotic ringspot disease caused by potato virus Y. The three factors studied in this work, which proved to influence the level of tuber necrosis reaction, were, first, the plant genotype, since varietal behaviour exhibited large differences; second, the virus genotype, since variations of virulence occurred between the four isolates tested; and third, the environmental conditions, as shown by the different rates of tuber necrosis obtained under contrasting conditions of temperature as much during the growing period as during storage. Three of the cultivars tested, Spunta, Maris Piper and Thalassa, failed to produce necrotic tubers, although infected with a virulent tuber-necrosing isolate. This result, following observations on the inheritance of the tuber necrosis trait, suggests that at least a major dominant gene controls this reaction in non-sensitive cultivars. On the other hand, the extreme resistance genes (Ry) provide a good resistance to virus infection, thus, preventing tuber necrosis under field conditions.

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Sequence polymorphism in the 5'NTR and in the P1 coding region of potato virus Y genomic RNA

Cited by 72 publications

References 52 publications

Three-dimensional model of the potyviral genome-linked protein.

Three-dimensional model of the potyviral genome-linked protein.

Nucleic acid-binding properties of a bacterially expressed potato virus Y helper component-proteinase

Effect of plant genotype, virus isolate and temperature on the expression of the potato tuber necrotic ringspot disease (PTNRD)

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