The nucleotide sequence of the genomic RNA of potato leafroll virus was determined and its genetic organization deduced. The RNA is 5882 nucleotides long and contains 6 open reading frames (ORFs) encoding proteins of 70, 70, 56, 28, 23 and 17 kDa. The putative genes for the coat protein (23 kDa) and the RNA-dependent RNA polymerase (70 kDa) were identified by interviral amino acid sequence homologies. For expression of the different ORFs, translational frameshift and readthrough events are proposed.cDNA cloning; Nucleotide sequence; Amino acid sequence homology; RNA virus, plant positive-strand; (Potato leafroll virus)
An Austrian isolate of potato virus yNTN, the causal agent of potato tuber necrotic ringspot disease (PTNRD), was serologically compared with seven Dutch PVY N isolates. Using polyclonal and monoclonal antibodies, it was found indistinguishable from PVY r~. Determination of the nucleotide sequence of the coat protein cistron and comparison of the deduced amino acid sequence with coat protein sequences of other potyviruses revealed a high level of homology with PVY s coat protein sequences. This confirmed the close taxonomic relationship of PVY Nrs with the PVY s subgroup of potato virus Y. PVY m~ is able to overcome all resistance genes known so far in commercial potato cultivars. Remarkably, transgenic PVY-protected tobacco plants are also resistant to PVY N~ infection upon mechanical and aphid-mediated inoculation. These experiments indicate that genetically engineered resistance offers great potential in protection of potato to new aggressive strains of PVY N.
Transgenic potato plants, cultivar Désir ée, were produced that contained the coat protein gene of potato leafroll luteovirus (PLRV). The transformed potato plants expressed the PLRV coat protein (CP) RNA sequences but accumulation of coat protein in transgenic tissues could not be detected. Upon inoculation with PLRV, the PLRV CP RNA expressing potato plants showed a reduced rate of virus multiplication.
The buoyant densities of bean yellow mosaic virus (BYMV) B25, pea mosaic virus (PMV) E198, lettuce mosaic virus (LMV), and potato virus yN (pVyN) were 1.318, 1.321, 1.330, and 1.326 g/ml, respectively. Their S values were 143, 140, 143, and 145 S. The particle morphology of BYMV B25, PMV E198, and LMV could reversibly be changed by magnesium ions. PVY N particles were broken in the presence of magnesium ions. The molecular weight of the coat protein subunit of the four viruses was 34,000 daltons. In many preparations also a 28,000 daltons component was present. This must be considered to be a breakdown product, derived from the 34,000 daltons component by proteolytic activity.
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