Internal cleavages of hepatitis C virus NS3 induced by P1 mutations at the NS3/4A cleavage site.

摘要: Despite being the focus of intensive investigation for its enzymatic activities and roles in HCV virus replication, little is known about internal processing NS3. Here we show that single mutations at P1 position NS3/4A junction lead to alternative cleavages. Among multiple novel cleavage products observed, there were two predominant species 12 kDa (p12) 67 (p67). This p12 consists NS4A a 6 long C-terminal region NS3 forms complex with The remaining corresponds p67 species. an protease-mediated intra-molecular event more interestingly can also be induced low concentrations one protease inhibitor examined. Our results led us propose model explaining observed functional role.