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Journal of Virology, January 1999, p. 11-18, Vol. 73, No. 1
Laboratory of Immunology,
Received 8 July 1998/Accepted 30 September 1998
Evidence from clinical and experimental studies of human and
chimpanzees suggests that hepatitis C virus (HCV) envelope glycoprotein E2 is a key antigen for developing a vaccine against HCV infection. To
identify B-cell epitopes in HCV E2, six murine monoclonal antibodies (MAbs), CET-1 to -6, specific for HCV E2 protein were generated by
using recombinant proteins containing E2t (a C-terminally truncated domain of HCV E2 [amino acids 386 to 693] fused to human growth hormone and glycoprotein D). We tested whether HCV-infected sera were
able to inhibit the binding of CET MAbs to the former fusion protein.
Inhibitory activity was observed in most sera tested, which indicated
that CET-1 to -6 were similar to anti-E2 antibodies in human sera with
respect to the epitope specificity. The spacial relationship of
epitopes on E2 recognized by CET MAbs was determined by surface plasmon
resonance analysis and competitive enzyme-linked immunosorbent assay.
The data indicated that three overlapping epitopes were recognized by
CET-1 to -6. For mapping the epitopes recognized by CET MAbs, we
analyzed the reactivities of CET MAbs to six truncated forms and two
chimeric forms of recombinant E2 proteins. The data suggest that the
epitopes recognized by CET-1 to -6 are located in a small domain of E2
spanning amino acid residues 528 to 546.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Identification of a Domain Containing B-Cell
Epitopes in Hepatitis C Virus E2 Glycoprotein by Using Mouse
Monoclonal Antibodies
*
Corresponding author. Mailing address: Laboratory of
Immunology, College of Pharmacy, Seoul National University,
Shillim-Dong, Kwanak-Gu, Seoul 151-742, Korea. Phone: 82-2-880-7860. Fax: 82-2-885-1373. E-mail: cykang{at}plaza.snu.ac.kr.
Journal of Virology, January 1999, p. 11-18, Vol. 73, No. 1
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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