Genomics-based identification of self-ligands with T cell receptor-specific biological activity

Immunol Rev. 2002 Dec;190:146-60. doi: 10.1034/j.1600-065x.2002.19011.x.

Abstract

Self-peptide/major histocompatibility complex (MHC) complexes profoundly influence the biology of T lymphocytes. They promote the selection of the T cell receptor (TCR) repertoire in the thymus, maintain the homeostasis of peripheral T cells prior to encounter with antigen, and modify the responsiveness of T cells to foreign antigens. In addition, they can serve as antigens for autoaggressive T cells that induce autoimmune diseases. The complete sequencing of the genomes of human, mouse, and many pathogenic organisms now provides us with a comprehensive list of all possible proteins that may be the source of foreign antigenic and self-peptides. A computational approach using profile-based similarity searches on potential self-MHC-binding peptides can be used to efficiently predict self-peptides with biological activities. The common feature of the identified peptides is similarity to antigen. Thus, self-peptides may form 'hazy' images of the universe of antigens that are used as templates to create and maintain the TCR repertoire.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Autoantigens / genetics*
  • Autoimmunity
  • Cell Differentiation
  • Genomics
  • H-2 Antigens / genetics
  • Humans
  • Major Histocompatibility Complex
  • Mice
  • Mice, Knockout
  • Mice, Transgenic
  • Molecular Mimicry
  • Ovalbumin / immunology
  • Phenotype
  • Receptors, Antigen, T-Cell / metabolism*
  • T-Lymphocytes / cytology
  • T-Lymphocytes / immunology

Substances

  • Autoantigens
  • H-2 Antigens
  • Receptors, Antigen, T-Cell
  • Ovalbumin