Immunological activity of covalently linked T-cell epitopes

Francesco Ria, Bosco M. C. Chan, Mark T. Scherer, John A. Smith, Malcolm L. Gefter

Risultato della ricerca: Contributo in rivistaArticolo in rivista

91 Citazioni (Scopus)


Immune response to proteins necessarily involve the recognition by T lymphocytes of a peptide or peptides derived from a a protein complexed with a major histocompatibility antigen. Th T-cell response of BALB/c mice to the bacteriophage lambda cI repressor protein (residues 1-102) is directed predominantly towards the epitope contained within a single peptide encompassing residues 12-26 (refs 1, 2). Similar phenomenon of immunodominance of a particular peptide have also been observed in other protein systems. The mechanism that have been suggested to account for the focusing of the T-cell response are partial deletion in the T cell repertoire, biased antigen processing, and competition for binding to the presenting molecule, the major histocompatibility complex encoded class II transplantation antigen. In a model system with a polypeptide containing two synthetically linked immunologically active epitopes, we now demonstrate the existence of a hierarchy between these epitopes, so that the immune response elicited is directed mainly towards the more immunogenic epitope whereas the less immunogenic epitope elicits little or no T cell reactivity. in addition the same hierarchy of dominance is also apparent when the polypeptide id used to induce tolerance in the periphery in adult mice.
Lingua originaleEnglish
pagine (da-a)381-383
Numero di pagine3
Stato di pubblicazionePubblicato - 1990


  • Animals
  • DNA-Binding Proteins
  • Epitopes
  • Histocompatibility Antigens Class II
  • Hybridomas
  • Immune Tolerance
  • Immunization
  • Mice
  • Mice, Inbred BALB C
  • Ovalbumin
  • Peptide Fragments
  • Repressor Proteins
  • T-Lymphocytes
  • Transcription Factors
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins


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