Molecular mimicry of hepatitis B surface antigen by an anti-idiotype-derived synthetic peptide

Michael W. Pride, Hong Shi, Jerry M. Anchin, D. Scott Linthicum, Philip T. LoVerde, Arvind Thakur, Yasmin Thanavala

Research output: Contribution to journalArticlepeer-review

59 Scopus citations


Monoclonal antibody 2F10 is an "internal-image" anti-idiotype (anti-id) antibody capable of mimicking the group-specific "a" determinant of human hepatitis B surface antigen (HBsAg). By mRNA sequencing and computer-assisted molecular modeling of monoclonal antibody 2F10, we identified a 15-amino acid region of the heavy-chain hypervariable region that has partial residue homology with sequences of the "a" determinant epitopes of HBsAg, We have established that a linear 15-mer peptide from a contiguous region on the anti-id antibody can (i) generate anti-HBsAg-specific antibodies when injected into mice, (ii) prime murine lymph node cells for in vitro HBsAg-specific T-cell proliferative responses, and (iii) stimulate in vitro human CD4+ T cells that were primed in vivo to HBsAg by natural infection with hepatitis B virus or vaccination with a commercially available HBsAg vaccine. Significantly, this peptide could also stimulate CD4+ T cells of human hepatitis B virus carriers. We conclude that a 15-mer peptide derived from the anti-id sequence can duplicate the B- and T-cell stimulatory activity of the intact anti-id antibody and the antigen that is mimicked, HBsAg.

Original languageEnglish (US)
Pages (from-to)11900-11904
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number24
StatePublished - 1992
Externally publishedYes


  • "a" determinant HBsAg
  • Epitope mimicry
  • Immune response
  • Molecular modeling
  • mRNA sequencing

ASJC Scopus subject areas

  • General


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