Biophysical mechanism of the scavenger site near T cell-presented epitopes

  • Lu S
  • Reyes V
  • Bositis C
 et al. 
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Abstract

We seek to identify consensus sequences in digested fragments of antigenic proteins regulating selection and major histocompatibility complex (MHC)-restricted presentation to T cells of epitopes within those fragments. One such pattern, of recurrent, hydrophobic sidechains forming a longitudinal hydrophobic strip when a sequence is coiled as an α-helix, is found in or near most T cell-presented epitopes. Such recurrent hydrophobicity may lead to protease-protected coiling of the fragment against endosomal membranes and transfer to MHC molecules. This concept leads to better identification of T cell-presented sequences and possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction. © 1992.

Author-supplied keywords

  • Antigen processing
  • MHC molecules
  • T cell-presented epitope
  • peptide vaccines
  • α-helix

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Authors

  • S. Lu

  • V. E. Reyes

  • C. M. Bositis

  • T. G. Goldschmidt

  • V. Lam

  • R. R. Torgerson

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