Evidence that polyoma polypeptide VP1 is a serine protease.
It has been shown that when purified polyoma (Py) virions are dissociated by incubation in 150 mM NaCl-50 mM Tris-HCl (pH 8.5) containing 1 mM EGTA and 3 mM DTT, two new polypeptides (MW 43.5K and 40K) are produced by proteolysis of virion polypeptide VP1. Proteolysis is blocked by diisopropyl fluorophosphonate (DFP) and phenylmethyl sulfonyl fluoride (PMSF), suggesting that the virion-associated enzyme is a serine protease. When Py virions were dissociated in the presence of radiolabeled DFP, only VP1 became labeled to any significant extent, which suggests that the protease activity is a property of this viral polypeptide and that the 43.5K and 40K species are produced by autodigestion.
D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000096:biosynthesis / Q000302:isolation & purification*; D007700:Kinetics; D008970:Molecular Weight; D011120:Polyomavirus / Q000201:enzymology*; D012697:Serine Endopeptidases; D014764:Viral Proteins / Q000096:biosynthesis / Q000302:isolation & purification*; D015678:Viral Structural Proteins; D014771:Virion / Q000201:enzymology
D014764:Viral Proteins; D015678:Viral Structural Proteins; D010450:Endopeptidases; D012697:Serine Endopeptidases