Abstract
A cDNA clone, C8-2, derived from nonstructural (NS) protein 5 region of hepatitis C virus (HCV) genome hasbeen isolated and was expressed in Escherichia coli as a fusion protein with β -galactosidase ( β -Gal). The recombinant protein, β -Gal/C8-2, was partially purified and used for detection of anti-HCV antibody by enzyme-linked immunosorbent assay (ELISA). Anti-C8-2 antibody was detected in 47% of patients with post-transfusion non-A, non-B (NANB) acute hepatitis and in 55% of patients with NANB chronic liver diseases. Of 1491 normal blood donors, ten (0.7%) were positive for anti-C8-2 antibody, and three of these ten samples were negative for anti-C100-3 antibody. HCV RNA was detected in one of these three samples. These results suggest that the recombinant protein containing C8-2 peptide may be useful as another nonstructural protein epitope for diagnosis of hepatitis C and screening of blood donors.
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