Disease relevance of PVYgp1

• Comparison of the PVY polyprotein sequence with that of other potyvirus polyproteins shows similarities in genome organization and a high level of identity along most of the polyprotein, except for the putative proteins flanking the helper component [1].
• The nt sequence and the predicted aa sequence of the polyprotein of PVY-H were analysed pairwise with the only available complete sequence of PVY strain N (PVYn) and with the partial sequences of different PVY strains, as well as with other potyviruses and potyvirus-related plant viruses [2].
• To test its proteolytic activity, the cDNA was modified so as to express the protease-polymerase-coat protein (CP) portion of PVY polyprotein in Escherichia coli [3].

High impact information on PVYgp1

• Other putative protein cleavage sites have been deduced by searching for consensus sequences and by analogy with the polyprotein of the tobacco vein mottling virus and of the tobacco etch virus [1].
• Phylogenetic analysis based on the polyprotein and coat protein amino acid sequences grouped WPMV, PVV, Pepper mottle virus and Potato virus Y in one cluster distinct from other potyviruses [4].
• The availability of such a clone is a prerequisite for any further study of the molecular biology of this group of viruses, as they are expressed into a self-processed primary polyprotein [5].
• Presence of a single open reading frame suggests that PVY-specific proteins are synthesized as a polyprotein precursor [6].
• Based on its nucleotide sequence, the cDNA was presumed to encode PVY protease responsible for the self-processing of polyprotein precursor expressed from PVY genome [3].

Analytical, diagnostic and therapeutic context of PVYgp1

• The result indicates that the CP gene cloned by PCR was functional and the PCR procedure was useful for producing biologically active cDNA clones from a single, long positive-sense RNA genome encoding a single, large polyprotein precursor, such as potyviruses [7].

References