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Objective: To construct the point mutation plasmids expressing HCV NS3/4A with different secondary structures at the N-terminus,and to analyze their serine protease activities. Methods: The point mutation plasmid constructs were generated by using the QuickChange site-directed mutagenesis kit with the backbone of M-H05-5 (A 1-1), and were named as subgroup A 1-2, A2-1, A2-2, B 1-1, B 1-2, B2-1,and B2-2 respectively. The transient expression of the constructs was investigated by immunofluorescence assay and Western blot analysis. The difference in in cis and in trans NS3 serine protease activity between each subgroup was determined by Western blot analysis. Luciferase reporter assay was used to observe the inhibitory effects of the constructs on RIG-I induced IFN-β promoter activity and on p53-dependent transcriptional activation. Results: The point mutation plasmid constructs were verified for the correct sequence by DNA sequencing. The imrnunofluorescence assay revealed 4 subcellular localization patterns of NS3, including dot-like staining, diffuse staining, doughnut-like staining, and rod-shape staining. Western blot analysis indicated that the incomplete cleavage of NS3/4A appeared in subgroups A2-1 and B2-1, indicating that the in cis NS3 serine protease activities of subgroup A2-1 and B2-1 were weaker when compared with the other subgroups. By using NS5A/SB△C as a substrate for NS3/4A serine protease, it was also found that the/n trans NS3 serine protease activities of subgroup A2-1 and B2-1 were also weaker compared the other subgroups. Differences in inhibitory effects of HCV NS3 on RIG-I induced IFN-β promoter activity and on p53-dependent transcriptional activation were also observed between subgroup A2-1, B2-1 and the other subgroups. Conclusion: The results suggest that subgroup A2-1 and B2-1 has weaker serine protease activities and weaker inhibitory activities on host cell functions than the other subgroups, which might be explained by the different secondary structure of the 120-aa sequence at N-terminus of NS3.

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篇名
来源期刊	南京医科大学学报(英文版)	学科
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年，卷（期）	2009,（4）	所属期刊栏目
研究方向		页码范围	257-264
页数	8页	分类号
字数		语种	英文
DOI