peptide mimotope of hepatitis C virus E2 protein is immunogenic in mice and block human anti-HCV sera

Conformational B-cell epitopes on the HCV E2 protein recognized by human antibodies were characterized by the use of a peptide mimotope named K1. K1 was identified by two HCV anti-E2 monoclonal antibodies (mAbs) following selection and purification of phage clones containing a 15-mer random peptide...

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Bibliographic Details
Published in:Journal of medical virology 2010-10, Vol.82 (10), p.1655-1665
Main Authors: El-Attar, L.M.R, Partidos, C.D, Howard, C.R
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal - immunology
Antibodies, Monoclonal - metabolism
Epitopes, B-Lymphocyte - genetics
Epitopes, B-Lymphocyte - immunology
Female
HCV
Hepacivirus - immunology
Hepatitis C Antibodies - blood
Hepatitis C Antibodies - metabolism
Humans
Mice
Mice, Inbred BALB C
mimotope
Peptide Library
Peptides - immunology
Protein Binding
therapeutic vaccine
Viral Envelope Proteins - genetics
Viral Envelope Proteins - immunology
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Summary:Conformational B-cell epitopes on the HCV E2 protein recognized by human antibodies were characterized by the use of a peptide mimotope named K1. K1 was identified by two HCV anti-E2 monoclonal antibodies (mAbs) following selection and purification of phage clones containing a 15-mer random peptide insert. Murine antisera to the mimotope K1 recognized the E2 protein. Five of eight human sera from patients who had cleared HCV recognized the K1 mimotope. Binding to E2 in four individuals with the capacity to block E2-CD81 interaction was inhibited by the mimotope K1. The results demonstrate that anti-E2 antibodies in sera from patients who have cleared HCV infection are directed against a conformational B-cell epitope on E2 that can be mimicked with linear synthetic peptides. These findings could have implications for vaccine design by employing linear mimotopes to direct B-cell responses against those specific E2 epitopes that may correlate with immunity. J. Med. Virol. 82:1655-1665, 2010. 2010 Wiley-Liss, Inc.
ISSN:0146-6615
1096-9071
DOI:10.1002/jmv.21857