Perpetuation of immunological memory through common MHC-I binding modes of peptidomimic and antigenic peptides

Biochem Biophys Res Commun. 2007 Dec 14;364(2):308-12. doi: 10.1016/j.bbrc.2007.10.005. Epub 2007 Oct 12.

Abstract

Understanding the molecular mechanisms of immunological memory assumes importance in vaccine design. We had earlier hypothesized a mechanism for the maintenance of immunological memory through the operation of a network of idiotypic and anti-idiotypic antibodies (Ab2). Peptides derived from an internal image carrying anti-idiotypic antibody are hypothesized to facilitate the perpetuation of antigen specific T cell memory through similarity in peptide-MHC binding as that of the antigenic peptide. In the present work, the existence of such peptidomimics of the antigen in the Ab2 variable region and their similarity of MHC-I binding was examined by bioinformatics approaches. The analysis employing three known viral antigens and one tumor-associated antigen shows that peptidomimics from Ab2 variable regions have structurally similar MHC-I binding patterns as compared to antigenic peptides, indicating a structural basis for memory perpetuation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Anti-Idiotypic / chemistry*
  • Antibodies, Anti-Idiotypic / immunology
  • Antigens, Viral / chemistry*
  • Antigens, Viral / immunology
  • Carcinoembryonic Antigen / chemistry*
  • Carcinoembryonic Antigen / immunology
  • Computational Biology
  • Epitopes
  • Genes, MHC Class I / immunology*
  • Immunoglobulin Variable Region / chemistry
  • Immunologic Memory*
  • Models, Molecular
  • Molecular Mimicry
  • Peptides / chemistry*
  • Peptides / immunology
  • Peptides / metabolism
  • Protein Binding

Substances

  • Antibodies, Anti-Idiotypic
  • Antigens, Viral
  • Carcinoembryonic Antigen
  • Epitopes
  • Immunoglobulin Variable Region
  • Peptides