Wild-type, but not mutant-type, p53 enhances nuclear accumulation of the NS3 protein of hepatitis C virus

By using vaccinia virus-T7 hybrid expression system, subcellular localization of the NS3 protein of hepatitis C virus was studied. Full-size NS3 (NS3F) and a carboxy-terminally truncated form (NS3 Delta C) were localized in the cytoplasm and the nucleus when expressed alone. However, NS3F and NS3 Delta C, but not amino- and carboxy-terminally truncated form (NS3 Delta N Delta C), were each co-localized with wild-type p53 almost exclusively in the nucleus upon co-expression. The wild-type p53-induced nuclear accumulation of NS3F was inhibited only partially by NS4A. When co-expressed with mutant-type p53, NS3F and NS3 Delta C were each co-localized with it exclusively in the cytoplasm. Taken together, the present results suggest that wild-type p53 enhances nuclear accumulation of NS3F and NS3 Delta C through the involvement of their amino-terminal sequences even in the presence of NS4A, and that mutant-type p53 inhibits their nuclear, and enhances their cytoplasmic, accumulation. (C) 1997 Academic Press