Abstract
Minor structural proteins are essential for virus infection, however their function in polyomavirus replication cycle are not fully understood. Three hydrofobic domain for VP2 and two domains for VP3 were predected to play important role in protein function.
Plasmid for expression of EGFP fusion variant of VP2 or VP3 and their deletion mutant were prepared. Their cytotoxicity, cellular localization and affinity to intracellular mebranes were examined.
Minor proteins fused with EGFP at their C-terminus were found to display properties similar to their nonfused, wild-type version. They induce apoptosis of mouse 3T3 cells dependent on caspase activation.
Despite of nuclear localisation signal a substantial subpopulation of VP2-EGFP and VP3-EGFP was detected in the cytoplasma, colocalising with intracellular membranes. Examining of deletion mutants of VP2 and VP3 revealed the importance of the hydrofobic domain 2 for their affinity to intracellural membranes.