Polyoma virus major capsid protein, VP1. Purification after high level expression in Escherichia coli.
We have expression-cloned in Escherichia coli the major polyoma virus capsid protein, VP1. Under the inducible control of the hybrid tac promoter, VP1 constituted between 2 and 3% of the total host cell protein. The expressed VP1 was purified to near homogeneity with initial yields to 10%. Optimal expression was temperature-dependent, and significant intracellular degradation could be demonstrated. The final product was obtained as one predominant isoelectric focusing species, without the pattern of post-translational modification seen invirus-infected eukaryotic cells. The purified VP1 from E. coli will be useful asa substrate for the purification of VP1 modification enzymes and in the study ofinter-VP1 oligomerization.