R. Ray et al., PEPTIDE IMMUNOGEN MIMICRY OF PUTATIVE E1 GLYCOPROTEIN-SPECIFIC EPITOPES IN HEPATITIS-C VIRUS, Journal of virology, 68(7), 1994, pp. 4420-4426
Hepatitis C virus (HCV) accounts for most cases of acute and chronic n
on-A and non-B hepatitis with serious consequences that may lead to he
patocellular carcinoma. The putative envelope glycoproteins (E1 and E2
) of HCV probably play a role in the pathophysiology of the virus. In
order to map the immunodominant domains of the El glycoprotein, two ep
itopes from amino acid residues 210 to 223 (P1) and 315 to 327 (P2) we
re predicted from the HCV sequence. Immunization of mice with the synt
hetic peptides conjugated to bovine serum albumin induced an antibody
response, and the antisera immunoprecipitated the E1 glycoprotein (sim
ilar to 33 kDa) of HCV expressed by recombinant vaccinia virus. A pane
l of HCV-infected human sera was also tested with the synthetic peptid
es by enzyme-linked immunosorbent assay for epitope-specific responses
. Of 38 infected serum samples, 35 (92.1%) demonstrated a spectrum of
reactivity to the P2 peptide. On the other hand, only 17 of 38 (44.7%)
serum samples were reactive to the P1 peptide. Strains of HCV exhibit
a striking genomic diversity. The predicted P1 epitope showed localiz
ation in the sequence-variable region, and the P2 epitope localized in
a highly conserved domain. Results from this study suggest that the E
1 glycoprotein of HCV contains at least two potential antigenic epitop
es. Synthetic peptides corresponding to these epitopes and antisera to
these peptides may serve as the monospecific immunological reagents t
o further determine the role of E1 glycoprotein in HCV infection.