By the use of recombinant baculoviruses, the -cleavage of hepatitis C virus (HCV) non-structural polyprotein was studied. The viral serine proteinase encoded by the NS3 gene was expressed efficiently in insect cells infected with a baculovirus recombined with HCV cDNA corresponding to amino acids 1046-1243 and the signal sequence of the rabies virus G protein. Coinfection studies showed the -cleavage activity of the expressed protein by the use of a recombinant producing NS5 as a substrate. We also found that the partially purified NS3 serine proteinase propared from the recombinant-infected cells could cleave NS5A/5B substrate. Characterization of the proteinase obtained will provide basic knowledge on processing of the HCV polyprotein.


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