Expression and purification of an active, full-length hepatitis C viral NS4A
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- Title
- Expression and purification of an active, full-length hepatitis C viral NS4A
- Authors
- Back, SH; Kim, JE; Rho, J; Hahm, B; Lee, TG; Kim, EE; Cho, JM; Jang, SK
- Date Issued
- 2000-11
- Publisher
- ACADEMIC PRESS INC
- Abstract
- The nonstructural protein 3 (NS3) of the hepatitis C virus (HCV) is a bifunctional protein with protease and helicase activities. Nonstructural protein 4A (NS4A) is preceded by NS3 and augments the proteolytic activity of NS3 through protein-protein interaction. The central domain of NS4A has been shown to be sufficient for the enhancement of the NS3 protease activity. However, investigations on the roles of the N-terminal and the C-terminal regions of NS4A have been hampered by the difficulty of purification of full-length NS4A, a polypeptide that contains highly hydrophobic amino acid residues. Here we report a procedure by which one can produce and purify an active, full-length NS4A using maltose-binding protein fusion method. The full-length NS4A fused to the maltose binding protein is soluble and maintains its NS3 protease-enhancing activity. (C) 2000 Academic Press.
- Keywords
- NON-B-HEPATITIS; NON-A; HEPATOCELLULAR-CARCINOMA; MAMMALIAN-CELLS; SERINE-PROTEASE; VIRUS GENOME; NS3; PHOSPHORYLATION; PROTEINASE; ANTIBODIES
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/19809
- DOI
- 10.1006/prep.2000.1301
- ISSN
- 1046-5928
- Article Type
- Article
- Citation
- PROTEIN EXPRESSION AND PURIFICATION, vol. 20, no. 2, page. 196 - 206, 2000-11
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