T Cell Epitope Hierarchy in Experimental Autoimmune Models

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

Abstract

During the course of an autoimmune inflammation the initial immune response focuses on dominant antigenic determinant(s). Endogenous self-priming subsequently leads to recognition of diverse cryptic epitopes of the same antigen (epitope spreading). Factors dictating epitope dominance/crypticity include thymic antigen expression, alternative splicing, thymic antigen processing and competitive interactions of antigenic peptides with self major histocompatibility complex, post-translational modifications, etc. Data from the experimental autoimmune encephalomyelitis model provided key insights into the rules governing establishment of epitope hierarchy. The chapter also summarizes data coming from the autoimmune aggrecan-induced murine arthritis model that suggest a significant role of glycosylation in establishment of epitope hierarchy. The initial immune response (focusing on the N-terminal G1 domain of aggrecan) later spreads to the C-terminal G3 domain. Intriguingly, both N- and C-terminal globular domains of aggrecan carry minimal glycosylation as compared with the long central carbohydrate attachment region, the epitopes of which are recognized only in acute arthritis.

Original languageEnglish
Title of host publicationImmunogenomics and Human Disease
PublisherJohn Wiley & Sons, Ltd
Pages327-349
Number of pages23
ISBN (Print)9780470015308
DOIs
Publication statusPublished - May 16 2006

Keywords

  • Alternative splicing
  • Autoimmune inflammation
  • Destructive processing
  • Dual TCR expression
  • Endogenous self-priming
  • Immunodominance
  • Intramolecular epitope spreading
  • Superagonist ligands
  • Supercryptic epitopes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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  • Cite this

    Buzas, E. (2006). T Cell Epitope Hierarchy in Experimental Autoimmune Models. In Immunogenomics and Human Disease (pp. 327-349). John Wiley & Sons, Ltd. https://doi.org/10.1002/0470034092.ch14