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J Gen Virol 76 (1995), 985-993; DOI 10.1099/0022-1317-76-4-985
© 1995 Society for General Microbiology
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Identification of the protease domain in NS3 of hepatitis C virus

Dae Sung Han1, Bumsuk Hahm1, Hyune-Mo Rho2 and Sung Key Jang1,*

1 Department of Life Science, Pohang University of Science and Technology, San31 Hyojadong, Pohang, Kyungbuk 790-784
and2 Department of Molecular Biology and Research Center for Cell Differentiation, Seoul National University, Seoul 151-742, Korea

NS3 of hepatitis C virus (HCV) is a serine protease that carries out the proteolytic processing of the nonstructural proteins of the HCV polyprotein. Deletion analysis of the N terminus of NS2,3,4 fusion protein revealed that the N-terminal boundary of the active protease resides between amino acids 1050 and 1083. The processing patterns of internal deletion mutants of NS2,3,4 indicated that the C terminus of the enzymically active protease resides between amino acids 1115 and 1218. The N- and C-terminal boundaries of the protease were also confirmed by determining the trans-cleavage activity of internally deleted NS3,4. NS3 protease activity was inhibited by Cu2+ but was slightly enhanced by Zn2+. This report provides a possible approach for development of antiviral agents based on protease inhibitors.

* Author for correspondence. Fax +82 562 279 2199. e-mail sungkey@vision.postech.ac.kr.internet

Received 23 May 1994; accepted 22 November 1994.


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