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Background The target of the study is Potato virus A (PVA, genus Potyviridae) and its genomelinked protein (VPg). Most of the PVA proteins are multifunctional, interacting with each other and with host proteins. Many of the functions are still unclear and some completely unknown. VPg is a 23 kDa protein interacting for example with viral polymerase. It has NTP-binding and nuclear localization signals overlapping with each other in the N-terminal end of the protein. Growing evidence shows that genome-linked proteins belong to a class of natively unfolded proteins [1]. Descriptive for this class is regions without fixed structure in the correctly folded and ready-made protein. Interactions between the unfolded region and its natural substrate usually launches folding but structural changes can be regulated also by other reactions such as phosphorylation.

Potato virus A genome-linked protein is a natively unfolded protein