48-mer synthetic peptide analogue of the hepatitis B virus "a" determinant induces an anti-HBs antibody response after a single injection
An extended (48 amino acid) synthetic peptide analogue of the hepatitus B virus (HBV) S protein (HBsAg) ‘a’ determinant has been produced by using 9‐fluorenylmethoxycarbonyl (fmoc) chemistry and a low substitution polystyrene resin as the solid phase support. This peptide (S121/48) elicited a sustai...
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Published in | Journal of medical virology Vol. 62; no. 2; pp. 159 - 166 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
New York
John Wiley & Sons, Inc
01.10.2000
Wiley-Liss |
Subjects | |
Online Access | Get full text |
ISSN | 0146-6615 1096-9071 |
DOI | 10.1002/1096-9071(200010)62:2<159::AID-JMV6>3.0.CO;2-X |
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Summary: | An extended (48 amino acid) synthetic peptide analogue of the hepatitus B virus (HBV) S protein (HBsAg) ‘a’ determinant has been produced by using 9‐fluorenylmethoxycarbonyl (fmoc) chemistry and a low substitution polystyrene resin as the solid phase support. This peptide (S121/48) elicited a sustained anti‐peptide antibody response in BALB/c (H‐2d) mice when immunised with Freund's complete adjuvant (FCA). Cross‐reactive, anti‐HBs antibodies were induced, directed against a significant proportion of the conformationally restrained epitope repertoire on the native HBsAg particles. Similar responses were obtained by injection of guinea pigs, a species known both to be exquisitely sensitive to HBsAg and to produce a wide range of B cell responses to HBsAg antigens. Taken together, these data show for the first time, that a synthetic peptide mimicking conformational epitopes can be produced by chemical synthesis and can be used to induce significant titres of anti‐HBs antibodies after a single injection. This immunogen has considerable potential for incorporation into novel delivery systems, e.g., microspheres, thus offering the potential of a controlled release, single dose hepatitis B vaccine. J. Med. Virol. 62:159–166, 2000. © 2000 Wiley‐Liss, Inc. |
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Bibliography: | istex:38CD5B5FE63E5A8784FAF1D33954BFCA6F99FC26 ark:/67375/WNG-RV1ZJWKW-H ArticleID:JMV6 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0146-6615 1096-9071 |
DOI: | 10.1002/1096-9071(200010)62:2<159::AID-JMV6>3.0.CO;2-X |