Induction of the human protein P56 by interferon, double-stranded RNA, or virus infection.

摘要: Abstract P56 is the most abundant protein induced by interferon (IFN) treatment of human cells. To facilitate studies on its induction pattern and cellular functions, we expressed recombinant as a hexahistidine-tagged in Escherichia coli purified it to apparent homogeneity using affinity chromatography. A polyclonal antibody raised against this was used show that primarily cytoplasmic protein. Cellular expression transfection did not inhibit replication vesicular stomatitis virus encephalomyocarditis virus. synthesis rapidly IFN-β, had half-life 6 h. IFN-γ or poly(A) + could induce protein, but poly(I)–poly(C) an 85-bp synthetic double-stranded RNA efficiently it. Similarly, infection GRE cells, which are devoid type I IFN genes, virus, Sendai caused induction. Surprisingly, also mutant cell line P2.1, cannot respond either IFN-α/β RNA. Induction P2.1 cells parental U4C preceded activation IRF-3 judged translocation nucleus from cytoplasm.