Figure 6
Co-chaperone protein BAG-1 regulate anti-HCV activity of tylophorine analogs. (a) DCB-3503 treatment decreased interaction of co-chaperone protein BAG-1 and Hsc70. Huh-luc/neo-ET cells were transiently transfected with HA- BAG-1 plasmid. The cells were treated with 30 nM DCB-3503 48 hours after transfection. Hsc70-associated HA-BAG-1 was immunoprecipitated with Hsc70 antibody as shown in Fig. 5a. Protein levels of HA-BAG-1 and Hsc70 were analyzed by Western blot. Huh-luc/neo-ET cells were transiently transfected in a six-well plate with 400 ng HA- BAG-1 plasmid or empty vector alone or in combination with (b) 30 nM DCB-3503, or (c) 3 nM rac-cryptopleurine for 36 hours. Levels of HCV RNA, NS3, NS5A, and HA-BAG-1 were analyzed by real-time PCR and Western blot, respectively. β-Actin served as the internal loading control. Results are representative of at least three independent experiments and presented as mean ± SD. P values are labeled on the graph.
