Disease relevance of PlPVgp1

• The effect of different protease inhibitors on the proteolytic processing of the plum pox potyvirus (PPV) polyprotein has been analyzed [1].
• The NIa-like protein of plum pox virus is a protease with high sequence specificity that is autocatalytically released from the viral polyprotein [2].
• Mutational analysis of plum pox potyvirus polyprotein processing by the NIa protease in Escherichia coli [3].
• The CI-6K2 polyprotein was observed in the baculovirus system and in infected plant cells [4].
• Molecular genetic analysis of a plant virus polyprotein cleavage site: a model [5].

High impact information on PlPVgp1

• Nuclear inclusion protein a (Nla) protease of turnip mosaic potyvirus is responsible for the processing of the viral polyprotein into functional proteins [6].
• Processing of the plum pox virus polyprotein at the P3-6K1 junction is not required for virus viability [7].
• The expression of potyvirus genomic RNA takes place through translation of its unique long and functional open reading frame into a large polyprotein that undergoes extensive proteolytic processing [8].
• The RNA genome of tobacco etch virus (TEV) is expressed as a polyprotein which is co- and post-translationally processed by viral encoded proteinases [5].
• Upon transfection of protoplasts with this construct, HC-Pro was expressed as part of the RNA2 encoded polyprotein from which it was fully processed [9].

Associations of PlPVgp1 with chemical compounds

• The TVBMV coat protein is processed from a larger polyprotein by cleavage at a Gln/Gly dipeptide, which is followed closely by the aphid transmission DAG triplet [10].

References