FIG. 1.
Schematic design of chimeric HCV NS3 protease-dependent BVDV and Npro-null BVDV. (A) Genome organization of BVDV. (B and C) Genome structures of the HCV NS3 protease-dependent BVDV (PH/B) and the mutant chimeric BVDV with an inactive HCV NS3 protease (PH/B(S139A), respectively. (D) Genome organization of BVDV−Npro. The shaded and open boxes represent BVDV structural and nonstructural polyproteins, respectively. The black boxes represent the HCV NS3 protease domain (residues 3 to 181). The open arrow indicates the cleavage site between the capsid (C) and Erns of BVDV by host signal peptidase. The arrows with dotted and solid lines show the cis-cleavages of Npro of BVDV and HCV NS3 protease, respectively. Inactive HCV NS3 protease was generated by alanine substitution of serine 139 (vertical line with S139A). In panel B the amino acid sequences of the HCV NS4A, the NS5A-NS5B junction between HCV NS3 protease, and BVDV C are indicated by single-letter amino acid codes. The cleavage site of HCV NS3 protease is marked by a solid arrow.